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Academic literature on the topic 'Recombinant protein'

Author: Grafiati

Published: 4 June 2021

Last updated: 15 June 2025

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Journal articles on the topic "Recombinant protein"

Niazi, Sarfaraz K., and Matthias Magoola. "mRNA and Synthesis-Based Therapeutic Proteins: A Non-Recombinant Affordable Option." Biologics 3, no. 4 (2023): 355–79. http://dx.doi.org/10.3390/biologics3040020.

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Recombinant technology has been around for nearly three quarters of a century and has revolutionized protein therapy. However, the cost of developing recombinant therapeutic proteins and the manufacturing infrastructure keeps their cost unaffordable for most patients. Proteins are produced in the body via messenger RNA (mRNA) translation. This process can be readily replicated through administering a chemical nucleic acid product to manufacture the same protein recombinantly. The progress made in creating these proteins ex vivo in a cell-free system also offers a lower-cost option to produce therapeutic proteins. This article compares these alternative methods for recombinant protein production, assessing their respective advantages and limitations. While developers and regulatory agencies may encounter significant challenges in navigating product approval, including many unresolved intellectual property issues, these technologies are now proven and offer the most logical solution to making therapeutic proteins accessible to most patients.

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Rodrigues, M., S. Li, K. Murata, et al. "Influenza and vaccinia viruses expressing malaria CD8+ T and B cell epitopes. Comparison of their immunogenicity and capacity to induce protective immunity." Journal of Immunology 153, no. 10 (1994): 4636–48. http://dx.doi.org/10.4049/jimmunol.153.10.4636.

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Abstract We compared the effectiveness of several recombinant influenza and vaccinia viruses to induce a malaria-specific immune response. The CD8+ T cell epitope of the circumsporozoite (CS) protein of Plasmodium yoelii, a rodent malaria parasite, was expressed in two distinct influenza virus proteins, the hemagglutinin and the neuraminidase. These recombinant viruses were found to be equally efficient at inducing CS-specific CD8+ T cells in mice. A third recombinant virus, which expresses a B cell epitope of the CS protein, induced neutralizing anti-sporozoite Abs. Expression in the same recombinant virus of the CD8+ T cell epitope and of the B cell epitope did not impair the capacity of this recombinant virus to induce malaria-specific CD8+ T cells and neutralizing Abs. The immunogenicity of a vaccinia virus, expressing the entire CS protein, was compared with that of a highly attenuated vaccinia strain expressing the same protein and with that of another vaccinia virus expressing only the CD8+ T cell epitope. All three vaccinia virus recombinants elicited CS-specific CD8+ cells and a potent inhibitory response against pre-erythrocytic stages of malaria parasites. Optimal levels of anti-sporozoite Abs, inhibition of liver stage development, and protection against malaria infection resulted from repeatedly immunizing the animals with recombinant influenza viruses followed by boosters with a recombinant vaccinia virus. These findings support the concept that live viral vectors expressing the appropriate proteins and/or epitopes can be used as promising vaccine candidates.

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Astuti, R. W., N. Wijayanti, and A. Haryanto. "Expression of Recombinant Fusion Protein from Local Isolate of Newcastle Disease Virus and Antibody Response to Recombinant Fusion Protein in Broiler Chickens Post-Vaccination." Journal of the Indonesian Tropical Animal Agriculture 45, no. 2 (2020): 78–90. http://dx.doi.org/10.14710/jitaa.45.2.78-90.

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This research aimed to express and purify the recombinant Fusion (F) protein of Newcastle Disease Virus (NDV) from a local isolate in Galur, Kulon Progo, Indonesia (0663/04/2013) from recombinant vector plasmid pBT7-N-His F, and to study the antibody response in the broiler sera which were injected with pure recombinant F protein compared with treated broilers that were vaccinated with commercial inactive NDV vaccines and control broilers without vaccination. The results showed that the recombinant F protein of NDV was successfully expressed, purified and visualized by SDS-PAGE with Coomassie Brilliant Blue staining and Westernblotting methods as a specific recombinant F protein with a molecular weight of 28 kDa. The pure recombinant F protein then was injected into broilers to determine the antibody response in broiler serum. Indirect ELISA showed that the production of antibodies was high in F protein vaccinated groups in comparison with other treated and control groups. The recombinant F protein has potential to be developed as a recombinant vaccine candidate after truncating the 6x His-tag part to obtain higher antibody respond if compared with antibody production in broiler serum post vaccinated with some commercially available broiler vaccines.

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Jawad, J., R. W. Astuti, A. Haryanto, and N. Wijayanti. "Antibody response to Newcastle disease virus recombinant fusion protein in post-vaccinated laying hens." Journal of the Indonesian Tropical Animal Agriculture 48, no. 1 (2022): 20–27. http://dx.doi.org/10.14710/jitaa.48.1.20-27.

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This research was aimed to analyze antibody response in laying hens post vaccinated by Newcastle Disease Virus (NDV) recombinat Fusion (F) protein which has been succesfully expressed from the F gene of local isolates of NDV from Kulon Progo strain (0663/04/2013), Yogyakarta, Indonesia. The F gene cloned into expression vector plasmid pBT7-N-His. Two types of NDV recombinant vaccine, a concentrated and pure F recombinant protein were used for vaccination. A concentrated recombinant F protein was collected from the centrifugal ultrafiltration process and a pure recombinant F protein was collected from the electroeluted process. Recombinant F protein of NDV was successfully expressed, purified, and visualized by Sodium Dodecyl Sulphate–Polyacrylamide Gel Electrophoresis (SDS-PAGE) with Coomassie Brilliant Blue staining with a molecular weight of 28 kDa. All two types of recombinant F vaccines and a commercial live vaccine as a positive control were injected two times at 14 and 18th weeks old laying hens to analyze the antibody response in serum. In comparison with a commercial live NDV vaccine, indirect Enzyme-linked Immunosorbent Assay (ELISA) revealed that antibody responses were high in both recombinant F protein vaccinated groups. In conclusion, the recombinant F protein has the potential to be developed as a recombinant vaccine candidate to obtain a higher antibody response in laying hens compared to commercially available live NDV vaccines.

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Ferrari, Luca, and Stefan G. D. Rüdiger. "Recombinant production and purification of the human protein Tau." Protein Engineering, Design and Selection 31, no. 12 (2018): 447–55. http://dx.doi.org/10.1093/protein/gzz010.

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Abstract Tau protein is a microtubule-stabilising protein whose aggregation is linked to Alzheimer’s Disease and other forms of dementia. Tau biology is at the heart of cytoskeletal dynamics and neurodegenerative mechanisms, making it a crucial protein to study. Tau purification, however, is challenging as Tau is disordered, which makes it difficult to produce in recombinant system and is degradation-prone. It is thus challenging to obtain pure and stable preparations of Tau. Here, we present a fast and robust protocol to purify Tau recombinantly in Escherichia coli. Our protocol allows purifying Tau either tag-less or FLAG-tagged at its N-terminus, and Tau fragments of interest. By exploiting a cleavable affinity tag and two anion exchange columns, we obtained Tau preparations of high purity, stable and suitable for in vitro studies, including aggregation experiments that resemble neurodegenerative processes.

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Lewis, Peter. "Recombinant protein drugs." British Journal of Clinical Pharmacology 53, no. 4 (2002): 411. http://dx.doi.org/10.1046/j.1365-2125.2002.01571.x.

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Yu, Xue-Jie, Patricia A. Crocquet-Valdes, Louis C. Cullman, Vsevolod L. Popov, and David H. Walker. "Comparison of Ehrlichia chaffeensisRecombinant Proteins for Serologic Diagnosis of Human Monocytotropic Ehrlichiosis." Journal of Clinical Microbiology 37, no. 8 (1999): 2568–75. http://dx.doi.org/10.1128/jcm.37.8.2568-2575.1999.

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Diagnosis of human monocytotropic ehrlichiosis (HME) generally depends on serology that detects the antibody response to immunodominant proteins of Ehrlichia chaffeensis. Protein immunoblotting was used to evaluate the reaction of the antibodies in patients’ sera with the recombinant E. chaffeensis 120- and 28-kDa proteins as well as the 106- and the 37-kDa proteins. The cloning of the genes encoding the latter two proteins is described in this report. Immunoelectron microscopy demonstrated that the 106-kDa protein is located at the surfaces of ehrlichiae and on the intramorular fibrillar structures associated with E. chaffeensis. The 37-kDa protein is homologous to the iron-binding protein of gram-negative bacteria. Forty-two serum samples from patients who were suspected to have HME were tested by immunofluorescence (IFA) using E. chaffeensis antigen and by protein immunoblotting using recombinant E. chaffeensisproteins expressed in Escherichia coli. Thirty-two serum samples contained IFA antibodies at a titer of 1:64 or greater. The correlation of IFA and recombinant protein immunoblotting was 100% for the 120-kDa protein, 41% for the 28-kDa protein, 9.4% for the 106-kDa protein, and 0% for the 37-kDa protein. None of the recombinant antigens yielded false-positive results. All the sera reactive with the recombinant 28- or the 106-kDa proteins also reacted with the recombinant 120-kDa protein.

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Koval, Olga, Galina Kochneva, Anastasiya Tkachenko, et al. "Recombinant Vaccinia Viruses Coding Transgenes of Apoptosis-Inducing Proteins Enhance Apoptosis But Not Immunogenicity of Infected Tumor Cells." BioMed Research International 2017 (2017): 1–14. http://dx.doi.org/10.1155/2017/3620510.

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Genetic modifications of the oncolytic vaccinia virus (VV) improve selective tumor cell infection and death, as well as activation of antitumor immunity. We have engineered a double recombinant VV, coding human GM-CSF, and apoptosis-inducing protein apoptin (VV-GMCSF-Apo) for comparing with the earlier constructed double recombinant VV-GMCSF-Lact, coding another apoptosis-inducing protein, lactaptin, which activated different cell death pathways than apoptin. We showed that both these recombinant VVs more considerably activated a set of critical apoptosis markers in infected cells than the recombinant VV coding GM-CSF alone (VV-GMCSF-dGF): these were phosphatidylserine externalization, caspase-3 and caspase-7 activation, DNA fragmentation, and upregulation of proapoptotic protein BAX. However, only VV-GMCSF-Lact efficiently decreased the mitochondrial membrane potential of infected cancer cells. Investigating immunogenic cell death markers in cancer cells infected with recombinant VVs, we demonstrated that all tested recombinant VVs were efficient in calreticulin and HSP70 externalization, decrease of cellular HMGB1, and ATP secretion. The comparison of antitumor activity against advanced MDA-MB-231 tumor revealed that both recombinants VV-GMCSF-Lact and VV-GMCSF-Apo efficiently delay tumor growth. Our results demonstrate that the composition of GM-CSF and apoptosis-inducing proteins in the VV genome is very efficient tool for specific killing of cancer cells and for activation of antitumor immunity.

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Kim, Yoo-Gon, Woo-Jong Lee, Chan-Hee Won, et al. "A study on short-term stability of recombinant protein A." Analytical Science and Technology 24, no. 3 (2011): 193–99. http://dx.doi.org/10.5806/ast.2011.24.3.193.

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Volkova, N. V., A. V. Ivanova, A. A. Isaeva, et al. "Obtaining Recombinant Antigens for the Development of Serological Diagnosis of Marburg Fever." Problems of Particularly Dangerous Infections, no. 4 (February 7, 2021): 47–52. http://dx.doi.org/10.21055/0370-1069-2020-4-47-52.

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Aim. Production of recombinant viral antigens of the main immunodominant proteins: glycoprotein (GPΔMLD), nucleoprotein (NP) and matrix protein (VP40) of the Marburg virus, as well as the study of their antigenic and immunogenic properties.Materials and methods. To create recombinant proteins GPΔMLD, NP and VP40 of the Marburg virus, synthesized nucleotide sequences encoding these proteins cloned into the pET21a expression vector were used. The immunogenic and antigenic properties of the obtained recombinant proteins were tested using a number of biomodels (mice, chickens, and guinea pigs).Results and discussion. Recombinant plasmids containing genes encoding proteins GPΔMLD, NP, VP40 of the Marburg virus, as well as Escherichia coli producing strains, with the yield of purified preparations of recombinant proteins GPΔMLD, NP, VP40 from one liter of culture fluid – 5, 10, and 10 μg were obtained, respectively. When mice are immunized, recombinant proteins GP, NP, and VP40 MARV induce the synthesis of high titer antibodies (recombinant proteins NP and VP40 – more than 409600, and recombinant protein GPΔMLD – 12800). Mouse antibodies specific to recombinant proteins interact in an enzyme-linked immunosorbent assay (ELISA) with the antigen of inactivated MARV. Antibodies of chickens immunized with virus-like particles containing the surface glycoprotein of the Marburg virus and antibodies of guinea pigs immunized with an experimental DNA vaccine containing the GPΔMLD MARV gene recognize the recombinant GPΔMLD protein and the viral protein in the inactivated MARV. The resulting recombinant proteins are immunogenic/antigenic and can be used for the development of enzymelinked immunosorbent assay systems.

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Dissertations / Theses on the topic "Recombinant protein"

Koscky, Paier Carlos Roberto 1983. "Padronização da expressão heterologa e de modelo de ensaio de atividade para a proteina quinase humana S6K." [s.n.], 2009. http://repositorio.unicamp.br/jspui/handle/REPOSIP/314787.

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Orientador: Nilson Ivo Tonin Zanchin Dissertação (mestrado) - Universidade Estadual de Campinas, Instituto de Biologia Made available in DSpace on 2018-08-14T12:40:52Z (GMT). No. of bitstreams: 1 KosckyPaier_CarlosRoberto_M.pdf: 3760581 bytes, checksum: 99331529324819b59a4360d60efd9b9a (MD5) Previous issue date: 2009 Resumo: A quinase de 70 kDa da proteína ribossomal S6, isoforma 1 (S6K1), é uma fosfoproteína implicada na regulação de genes relacionados ao controle da tradução em mamíferos e possui uma forma nuclear (a1) e uma citoplasmática (a2). A fosforilação do seu principal alvo, a proteína RPS6, tem sido comumente associada ao recrutamento seletivo dos 5'-TOP (5' tract of oligopyrimidine) mRNAs pela maquinaria de tradução, embora haja estudos contrariando esta hipótese. Devido às funções de seus demais alvos, S6K1 tem sido implicada na sobrevivência celular e em diversos outros processos, como crescimento, câncer e resistência à insulina. S6K1 é ativada por um mecanismo que envolve fosforilação seqüencial através da ativação das vias mTORC1 (complexo 1 do alvo da rapamicina em mamíferos) e PI3K (fosfoinositol-3 quinase). Como uma quinase da família AGC, S6K1 deve ser fosforilada por mTORC1 no resíduo Thr389 do domínio hidrofóbico e, em seguida, por PDPK1 (proteína quinase 1 dependente de fosfoinositol) no resíduo Thr229 da alça T do domínio catalítico. Estes eventos ocorrem somente após a fosforilação em diversos sítios do domínio auto-inibitório carboxiterminal, por mTORC1. O objetivo deste trabalho foi desenvolver um ensaio modelo para análise da função da S6K1 in vitro e utilizá-lo como ferramenta na elucidação do papel de proteínas adaptadoras da via de mTOR em interações com a S6K1. Para isso foi necessário produzir as proteínas recombinantes para ensaios de interação e para realização de um ensaio de atividade para a S6K1. Foram testados vários sistemas de expressão para Escherichia coli para produção das construções GST-S6K1a1-His6, GST-S6K1a2-His6 e GST-S6K1a2T389E?CT (forma a2 de S6K1 com a substituição T389E e o carboxiterminal truncado), GST-PDPK1 e GST-CDPDPK1 (domínio catalítico de PDPK1 fusionado a GST). A expressão das formas truncadas de S6K1 e PDPK1 foi mais eficiente em E. coli. Embora o rendimento tenha ficado muito aquém do esperado, foi suficiente para os ensaios de interação in vitro. Também foi feita a expressão em E. coli da região C-terminal da proteína RPS6, que é o substrato da S6K1, em fusão com a proteína D do fago ?. Posteriormente, foram montados sistemas de expressão das construções His6-S6K1a2T389E?CT e His6-CDPDPK1 em células de inseto, a partir de vetor de baculovírus. Constatou-se que essas construções são expressas na forma de fosfoproteínas em células de inseto. Ensaios de GST pull-down com GST-S6K1a2-His6 e GST-S6K1a2T389E?CT contra as duas isoformas da subunidade catalítica da PP2AC, His6-PP2ACa(maior) e His6-PP2ACa(menor), revelaram que His6-PP2ACa(maior) não interage com GST-S6K1a2-His6, embora interaja fortemente com GST-S6K1a2T389E?CT. Já a construção His6-PP2ACa(menor) interage fracamente com as construções GST-S6K1a2-His6 e GST-S6K1a2T389E?CT. Tomados em conjunto, os resultados sugerem que a presença do C-terminal não fosforilado de S6K1a2 impede a interação com PP2ACa(maior). PP2ACa(menor) comporta-se de forma completamente diferente da isoforma maior, pois a interação entre PP2ACa(menor) e S6K1a2 parece ser independente do carboxiterminal da quinase, visto que as quantidades de S6K1a2T389E?CT e de S6K1a2 inteira que interagem com PP2ACa(menor) são semelhantes. Esses resultados necessitam ainda serem confirmados in vivo. Outros experimentos de GST pull-down confirmaram que as construções de S6K1 não interagem com a4, embora interajam com TIPRL1. Se confirmado in vivo, esse resultado compõe um novo quadro na regulação coordenada entre mTOR1 e PP2A, do qual TIPRL1 parece participar. As construções genéticas e os sistemas de expressão gerados neste trabalho possibilitaram a obtenção dos reagentes necessários para analisar o mecanismo de regulação da quinase S6K1, mediado por proteínas regulatórias. Permitem também desenvolver uma série de experimentos, como busca de inibidores específicos para a S6K1, que dependem da reconstituição de ensaios de atividade in vitro com a S6K1 ativada. Contudo, o ensaio de atividade realizado não apresentou resultados satisfatórios e precisa ser desenvolvido. Abstract: The 70kDa ribosomal S6 protein kinase 1 (S6K1) is a phosphoprotein involved in the regulation of genes related to translational control in mammals. S6K1 shows distinct nuclear (a1) and cytoplasmic (a2) forms. Phosphorylation of the S6K1 best characterized target, the protein of the small ribosomal subunit (RPS6), has been generally associated to the selective recruitment of the 5'-TOP mRNAs (5' tract of oligopyrimidine) by the translational machinery, although there is still some controversy on this issue. Due to the function of its targets, S6K1 has been implicated in several cellular processes including cell growth, cancer and insulin resistance. S6K1 is activated by a mechanism of sequential phosphorylation following activation of the mTORC1 (mammalian target of rapamycin complex 1) and PI3K (phosphoinositide-3-kinase) pathways. As a kinase of the AGC family, S6K1 activation requires mTORC1 phosphorylation of residue Thr389 of the hydrophobic domain followed by PDPK1 (phosphoinositide dependent protein kinase 1) phosphorylation of residue Thr229 at the T loop of the catalytic domain. These take place only after phosphorylation by mTORC1 of several residues of the autoinhibitory C-terminal domain. The objective of this work was to develop an assay to analyze the function of S6K1 in vitro and use it as a tool in the discovering of the functions of regulators proteins of the mTOR cascade in interactions with S6K1. For these purposes, expression systems were constructed to produce the various recombinant proteins to be used in the interaction and activity assays. Several genetic constructions were tested in Escherichia coli for the production of GST-S6K1a1-His6, GST-S6K1a2-His6 and GST-S6K1a2T389E?CT (a2 form of S6K1 with the T389E substitution and truncated carboxiterminus), GST-PDPK1 and GST-CDPDPK1 (GST fusion protein of the catalytic domain of PDPK1). The truncated forms were expressed more efficiently in E. coli. Although the yield in E. coli was lower than expected, it was sufficient to perform interaction assays. The C-terminal domain of RPS6, a substrate for S6K1, was successfully expressed in E. coli as a fusion protein with the phage ? protein D. Subsequently, expression systems for production of His6-S6K1a2T389E?CT and His6-CDPDPK1 in insect cells were constructed using baculovirus vectors. It was found that these constructs are expressed in the form of phosphoproteins in insect cells. GST pull-down assays using GST-S6K1a2-His6 e GST-S6K1a2T389E?CT to test interaction with the PP2AC isoforms His6-PP2ACa(major) and His6-PP2ACa(minor) revealed that His6-PP2ACa(major) does not interact with GST-S6K1a2-His6, although it interacts strongly with GST-S6K1a2T389E?CT. On the other hand, His6-PP2ACa(minor) interacts weakly with both GST- S6K1a2-His6 and GST-S6K1a2T389E?CT. This finding suggests that the unphosphorylated C-terminal of S6K1a2 inhibits interaction with PP2ACa(major). His6-PP2ACa(minor) behaves differently form His6-PP2ACa(major). Its interaction with S6K1a2 seems to be independent of the C-terminal since the amounts of S6K1a2T389E?CT and S6K1a2 that interact with His6-PP2ACa(minor) are similar. Future work in vivo is required to confirm these results. GST pull-down assays confirmed that a4 does not interact with the constructions of S6K1, while TIPRL1 interacts with them. If confirmed in vivo, these results provides a new perspective for the coordinated regulation between mTOR1 and PP2A, which apparently involves also TIPRL1. The genetic constructions and expression systems established in this work allow the production of the reagents required to study the mechanism of S6K1 regulation mediated by adaptor proteins. They will also allow the development of experiments such as screening for specific S6K1 inhibitors, which depend on reconstitution of S6K1 activity assays using activated S6K1. Nevertheless, the activity assay performed did not yield satisfactory outcomes and must be improved. Mestrado Bioquimica Mestre em Biologia Funcional e Molecular

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Tse, Muk-hei. "Investigations on recombinant Arabidopsis acyl-coenzyme A binding protein 1." View the Table of Contents & Abstract, 2005. http://sunzi.lib.hku.hk/hkuto/record/B36427664.

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Tse, Muk-hei, and 謝牧熙. "Investigations on recombinant Arabidopsis acyl-coenzyme A binding protein 1." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2005. http://hub.hku.hk/bib/B36427664.

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Corgozinho, Carolina Nunes Costa. "Desenvolvimento de vacina baseada em sistema de liberação sustentada contendo proteína recombinante." Universidade de São Paulo, 2008. http://www.teses.usp.br/teses/disponiveis/60/60137/tde-31072009-083709/.

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No Brasil, e em outros paises de clima tropical, os carrapatos se tornaram um enorme problema economico de^$de que a industria do gado se desenvolveu. O carrapato Boophilus microplus, um dos artropodes mais importantes na veterinaria, causa efeitos direto, como suc,cao de sangue, e indireto, como a transmissao de uma grande variedade de patogenos que normalmente resulta em infec,c~es letais. As vacinas genicas contendo o antigeno Bm86, uma proteina ligada a membrana do intestino do carrapato B. microplus, representam uma alternativa atrativa aos acaricidas para controlar as infesta~oes por carrapatos em contrapartida aos inconvenientes produtos quimicos. Devido sua administra,cao ser feita em 4 doses no primeiro ano, seguida de refor,cos a cada seis meses, estas formula,coes vacinais nao s3c adequadas para paises com cria,cao extensiva de gado, como no Brasil. Visando uma libera~ao sustentada do antigeno Bm86, neste trabalho desenvolveuse uma vacina de dose unica baseada em microesferas polimericas. Para obter o padrao de liberac,ao desejavel, diferentes formula,coes e parametros de processo foram variados, como a composi,cao do polimero, a taxa entre os monomeros ^Uacido latico:acido glicolico\" e o tamanho das microparticulas. As formula,coes foram preparadas pelo metodo de emulsao multipla e evapora,cao do solvente. A formula~ao que melhor se enquadrou nos objetivos da vacina de dose unica foi preparada com PLGA 75:25, solu,cao 3% de PVA como estabilizante, agita,cao de 11000 rpm para forma,cao da emulsao primaria e de 800 rpm para forma,cao da emulsao multipla e evapora,cao do solvente. As particulas assim obtidas apresentaram um tamanho medio de 25 ,um, uma taxa de encapsula,cao maior que 90% e aproximadamente 50% da proteina foi liberada in vitro em 60 dias. Analises por SDS-PAGE e Westem Bloning revelaram que a proteina se manteve integra apos encapsula,cao. Os resultados da avalia,cao da imunogenicidade em bovinos mostraram que a formula,cao baseada em microesferas polimericas biodegradaveis e habil a conseguir, com uma unica dose, uma resposta imune similar aquela conseguida com tres doses das formula,coes convencionais da vacina de Bm86. In Brazil, and in others tropical countries, the ticks have become a huge economic problem since the industry of livestock has developed. Ticks and tick-borne diseases affect animal and human health and are the cause of significant economic losses. The cattle tick Boophilus microplus is one of the most important arthropods in veterinary. This tick species causes both direct effects, such as blood sucking, and indirect effects, such as transmission of a wide variety of pathogens, which usually result in lethal infections. The gene vaccines based on Bm86 antigen, a midgut membrane-bound protein of the cattle tick B. microplus, represent a good alternative to control tick infestations, compared to chemicals. However, due to these vaccine formulations need 4 doses over the first year with booster at each 6 months to be effective, they are not suitable for countries with extensive cattle raising, like Brazil. Aiming a sustained release of Bm86 antigen, in this work we developed a single shot vaccine based on Bm86 loaded polymeric microspheres. In order to obtain desired release patterns, different formulations and processing parameters were varied, for example, the composition of the polymer, the monomer ratio lactic acid:glycolic acid and the size of the microparticles. The formulations were prepared by solvent evaporation method based on double emulsion. The formulation that presented better result as single shot vaccine was prepared with PLGA 75:25, solution 3% of PVA as stabilizer, agitation of 11000 rpm to form the primary emulsion and 800 rpm to obtain the double emulsion and solvent evaporation. The particles thus obtained presented an average size of 25 m, encapsulation ratio greater than 90% and approximately 50% of the protein was released in vitro in 60 days. Analysis by SDSPAGE and Western Blot showed that the integrity of the protein remained after encapsulation. The immunogenic studies showed that the formulation based onbiodegradable polymeric microspheres is able to elicit, with a single dose, an immune response and protection similar to that attained with 3 doses of conventional Bm86 vaccine formulations.

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Ndabambi, Nonkululeko. "Recombinant expression of the pRb- and p53-interacting domains from the human RBBP6 protein for in vitro binding studies." Thesis, University of the Western Cape, 2004. http://etd.uwc.ac.za/index.php?module=etd&amp.

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The aim of this thesis was to produce DNA expression constructs and use them to investigate the feasibility of recombinantly expression proteins for future interaction studies between human RBBP6 and p53 and pRb proteins.

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Barua, Bipasha. "Design and study of Trp-cage miniproteins /." Thesis, Connect to this title online; UW restricted, 2005. http://hdl.handle.net/1773/8533.

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Bleckwenn, Nicole Aleece. "Protein production development with recombinant vaccinia virus." College Park, Md. : University of Maryland, 2004. http://hdl.handle.net/1903/1416.

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Thesis (Ph. D.) -- University of Maryland, College Park, 2004. Thesis research directed by: Chemical Engineering. Title from t.p. of PDF. Includes bibliographical references. Published by UMI Dissertation Services, Ann Arbor, Mich. Also available in paper.

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Morreale, Giacomo. "Processing of recombinant fusion protein and peptide." Thesis, University of Cambridge, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.615060.

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Pesarrodona, Roches Mireia. "Supramolecular organisation and biological properties of tumor targeted, self-assembling protein nanoparticles." Doctoral thesis, Universitat Autònoma de Barcelona, 2017. http://hdl.handle.net/10803/402365.

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Degut a la seva flexibilitat funcional i arquitectònica, l’ús de proteïnes recombinants formades per múltiples dominis representen una eina interesant pel desenvolupament de nanopartícules capaces de transportar fàrmacs de manera específica. Recentment, en el nostre grup, hem aplicat un nou sistema d’enginyeria pel desenvolupament de nanoparticles formades mitjançant l’oligomerització de proteïnes modulars. L’eficàcia selectiva i l’absència de toxicitat d’unes nanopartícules dirigides al càncer colorectal demostra la capacitat d’aquest enfoc biotecnològic. Un enfoc basat en l’ús de pèptids catiònics en els extrems terminal d’una proteïna modular que li confereix la capacitat d’interaccionar amb sí mateixa formant nanopartícules proteiques. Per tal d’explorar la flexibilitat d’aquest enfoc, hem desenvolupat dues nanopartícules proteiques, anomenades A5G27-GFP-H6 i FNI/II/V-GFP-H6, que reconeixen i internalitzen, de manera específica, cèl·lules que expressen el receptor CD44. Aquestes proteïnes modulars formen estructures anulars de 14 nm, estables en plasma capaces d’internalitzar a través d’endocitosis sense presentar toxicitat cel·lular. Aquestes nanopartícules específiques són una plataforma prometedora com a nanomedicines pel transport de fàrmacs o sondes pel diagnòstic i tractament d’afliccions relacionades amb CD44. Durant la producció recombinant microbiana, moltes proteïnes heteròlogues tendeixen a acumular-se en cossos d’inclusió. Tenint en compte la última descripció d’aquestes entitats, constitueixen una font de proteïna pràcticament pura. Tot i que s’han desenvolupat tècniques per l’obtenció de proteïna activa mitjançant l’ús de detergents solubilitzadors no desnaturalitzants de manera satisfactòria, és desconegut com aquests procediments afecten el procés d’oligomerització de nanopartícules proteiques. En aquesta tesi, hem analitzat quin impacte té, a nivell estructural i funcional, l’origen de la font proteica. Depenent de si les nanopartícules deriven de la fracció soluble o de la resolubilització dels cossos d’inclusió, s’obtenen diferents organitzacions supramoleculars amb comportaments funcionals diferenciats. Aquests resultats demostren la rellevància que té l’origen cel·lular del material quan parlem d’estructures proteiques complexes. Tot i que recentment s’ha demostrat que la bactèria hoste té una influencia directe en la estructura i el rendiment de les nanopartícules proteiques, es desconeix com els hi afecta l’ús de bactèries amb un perfil genètic diferent com soques deficients en xaperones o lliures de lipopolisacàrids. En aquesta tesi, s’ha investigat l’estructura de nanopartícules dirigides a CD44 o CXCR4 produïdes en diferents soques d’E.coli i com les característiques fisicoquímiques afecten la biointeracció d’aquestes nanopartícules. Els resultats demostres la robustesa dels patrons d’oligomerització d’aquestes nanopartícules dirigides a tumor i la influencia que té el perfil genètic microbià en la proporció de les diferents poblacions oligomèriques en el producte cru. Aquesta variabilitat, intrínseca de la bioproducció, tot i ser imprevisible o incontrolable, constitueix un ventall de nanomaterial. De manera exclusiva es pot seleccionar aquella població de nanopartícules amb les característiques funcionals i fisicoquímiques òptimes considerant l’aplicació per la qual s’han dissenyat. Recombinant multidomain protein building-blocks have demonstrated to be an appealing biotechnological approach for the development of cell-targeted, nanoscale drug carriers on account of protein functional and architectonic versatility. The colorectal tumor targeting efficacy as well as non-toxicity of T22-empowered nanoparticles validates the potential of the de novo engineering approach developed in our research group. An approach based on end-terminal cationic peptides as pleiotropic tags in self-assembling protein building blocks. In an attempt to explore the flexibility of this approach, we have developed two protein-only nanoparticles that specifically bind CD44-receptor, namely A5G27-GFP-H6 and FNI/II/V-GFP-H6. These designed building-blocks promote the formation of ring-shaped structures which are approximately 14 nm in size, stable in plasma that can internalise cells through endocytosis in absence of cell toxicity. These targeted protein nanoparticles, together with the stability and biodistribution of other tested multifunctional self-assembling protein nanoparticles, are promising platforms for the transport of drugs or imaging agents as nanomedicines for breast cancer or other CD44-linked afflictions. Referring to microbial cell factories, many of the recombinant proteins are likely accumulated in IBs upon induction stress; however, considering non-classical structure description of these protein build-ups they represent an abundant and pure protein source. Although active protein has been obtained from IBs through mild solubilisation procedures, it is still unknown how the recovery of active protein from IBs affects the self-assembling process into protein nanoparticles. Thus, we have analyse the impact on nanoparticle structure and functionality considering the protein material source (nanoparticles from the soluble cell fraction or resolubilised from IBs) of the developed CD44-targeted protein vehicles. We have identified altered supramolecular organisation and consequently distinct in vitro and in vivo performance of cell-targeted protein nanoparticles depending on material’s origin. It is a particularly important aspect regarding recombinant production of smart and complex protein structures Albeit it has been recently known that the bacterial host directly influence the architecture and the performance of the produced protein nanoparticles, how the genetic background of E. coli strains deficient of chaperons or LPS-free affect these protein assemblies has not been addressed. In this thesis we have investigated the fine structure of CXCR4 and CD44 targeted nanoparticles produced in different E. coli strains and how their physicochemical characteristics affect the nanoparticles’ biointeractions. Results illustrate the robustness of self-assembling patterns among tumor-targeted GFP nanoparticles and also the influence of genetic background of the producing cells on shifting the distribution of oligomeric population in the pooled material. The intrinsic variability derived from the bioproduction, although being unpredictable or uncontrollable, offers a scope of nanoparticulated material from where optimal population can be selected considering their ultimate application

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Comenale, Gabriela. "Expressão e purificação da proteína recombinante L2 do Papilomavírus bovino tipo-2 em sistema bacteriano." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/10/10132/tde-11102013-104819/.

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A papilomatose bovina é uma doença infectocontagiosa de ocorrência mundial, que assola o rebanho brasileiro, sem qualquer atitude efetiva de controle, e que tem como enfermidades associadas a tumores de bexiga hematúria enzoótica e tumores de trato digestório superior caraguatá, responsáveis por sensíveis perdas para a pecuária. Várias tentativas vacinais têm sido empreendidas com finalidades profiláticas ou terapêuticas, porém sem resultados eficazes. Esta situação se deve a aspectos relacionados à estrutura viral que dificultam uma manipulação eficiente para produção de produtos vacinais. Para que tais dados possam ser obtidos, faz-se necessário uma melhor compreensão da ação das proteínas recombinantes. A clonagem em vetores bacterianos para a expressão e purificação dessas proteínas serve a diferentes propósitos. Entre eles, a produção de insumos imunológicos, como testes diagnósticos ou mesmo vacinas. O presente projeto visou à expressão e purificação da proteína de capsídeo recombinante L2 de BPV-2. A proteína foi expressa em bactéria e tentou-se a purificação por coluna de afinidade; entretanto, problemas na purificação não possibilitaram a conclusão deste objetivo. Todas as abordagens e protocolos utilizados nesse trabalho são discutidos para contribuição ao conhecimento do processo. The bovine papillomatosis is an infectious disease of worldwide occurrence, plaguing the Brazilian herd, without any effective attitude control, and whose illnesses associated with bladder tumors \"enzootic hematuria\" and upper digestive tract tumors \"caraguatá\" sensitive responsible for losses to livestock. Several attempts have been undertaken vaccine with prophylactic or therapeutic purposes, but without effective results. This is due to issues related to viral structure that hinder efficient manipulation for production of vaccine products. In order to obtain such information, it is necessary better understanding of the action of recombinant proteins. The bacterial cloning vectors for the expression and purification of such proteins serve different purposes. Among them, the production of immune inputs, such as diagnostic tests or vaccines. This project aimed the expression and purification of recombinant L2 capsid protein of BPV-2. The protein was expressed in bacteria and purification was carried out by affinity column. However, difficulties in the purification process, impaired the full completion of this objective. All the attempted approaches and protocols were discussed and potential solutions proposed.

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Books on the topic "Recombinant protein"

Tuan, Rocky S. Recombinant Protein Protocols. Humana Press, 1997. http://dx.doi.org/10.1385/089603481x.

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Buckel, Peter, ed. Recombinant Protein Drugs. Birkhäuser Basel, 2001. http://dx.doi.org/10.1007/978-3-0348-8346-7.

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Bill, Roslyn M., ed. Recombinant Protein Production in Yeast. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-770-5.

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Gasser, Brigitte, and Diethard Mattanovich, eds. Recombinant Protein Production in Yeast. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9024-5.

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Jean, Garnier, ed. Introduction to proteins and protein engineering. Elsevier, 1986.

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Jean, Garnier, ed. Introduction to proteins and protein engineering. Elsevier, 1988.

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Hacker, David L., ed. Recombinant Protein Expression in Mammalian Cells. Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8730-6.

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Howard, John A., and Elizabeth E. Hood, eds. Commercial Plant-Produced Recombinant Protein Products. Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-662-43836-7.

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Hacker, David L., ed. Recombinant Protein Expression in Mammalian Cells. Springer US, 2024. http://dx.doi.org/10.1007/978-1-0716-3878-1.

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S, Tuan Rocky, ed. Recombinant protein protocols: Detection and isolation. Humana Press, 1997.

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Book chapters on the topic "Recombinant protein"

Fothergill-Gilmore, Linda A. "Recombinant Protein Technology." In Protein Biotechnology. Humana Press, 1993. http://dx.doi.org/10.1007/978-1-59259-438-2_13.

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Weissmann, Charles. "Recombinant interferon - the 20th anniversary." In Recombinant Protein Drugs. Birkhäuser Basel, 2001. http://dx.doi.org/10.1007/978-3-0348-8346-7_1.

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Hofschneider, Peter Hans, and Kenneth Murray. "Combining science and business: from recombinant DNA to vaccines against hepatitis B virus." In Recombinant Protein Drugs. Birkhäuser Basel, 2001. http://dx.doi.org/10.1007/978-3-0348-8346-7_2.

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Brownlee, George G., and Paul L. F. Giangrande. "Clotting factors VIII and IX." In Recombinant Protein Drugs. Birkhäuser Basel, 2001. http://dx.doi.org/10.1007/978-3-0348-8346-7_3.

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Welte, Karl, and Erich Platzer. "Colony-stimulating factors: altering the practice of oncology." In Recombinant Protein Drugs. Birkhäuser Basel, 2001. http://dx.doi.org/10.1007/978-3-0348-8346-7_4.

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Collen, Désiré, and H. Roger Lijnen. "Tissue-type plasminogen activator: helping patients with acute myocardial infarction." In Recombinant Protein Drugs. Birkhäuser Basel, 2001. http://dx.doi.org/10.1007/978-3-0348-8346-7_5.

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Gillies, Stephen D. "Designing immunocytokines: genetically engineered fusion proteins for targeted immune therapy." In Recombinant Protein Drugs. Birkhäuser Basel, 2001. http://dx.doi.org/10.1007/978-3-0348-8346-7_6.

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Burke, Paul A., and Scott D. Putney. "Improving protein therapeutics: the evolution of the modern pharmacopoeia." In Recombinant Protein Drugs. Birkhäuser Basel, 2001. http://dx.doi.org/10.1007/978-3-0348-8346-7_7.

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Friedmann, Theodore. "Principles of gene transfer and foreign protein expression for human gene therapy." In Recombinant Protein Drugs. Birkhäuser Basel, 2001. http://dx.doi.org/10.1007/978-3-0348-8346-7_8.

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Buntru, Matthias, Simon Vogel, Ricarda Finnern, and Stefan Schillberg. "Plant-Based Cell-Free Transcription and Translation of Recombinant Proteins." In Recombinant Proteins in Plants. Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2241-4_8.

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AbstractPlant cell-free lysates contain all the cellular components of the protein biosynthesis machinery, providing an alternative to intact plant cells, tissues, and whole plants for the production of recombinant proteins. Cell-free lysates achieve rapid protein production (within hours or days) and allow the synthesis of proteins that are cytotoxic or unstable in living cells. The open nature of cell-free lysates and their homogeneous and reproducible performance is ideal for protein production, especially for screening applications, allowing the direct addition of nucleic acid templates encoding proteins of interest, as well as other components such as enzyme substrates, chaperones, artificial amino acids, or labeling molecules. Here we describe procedures for the production of recombinant proteins in the ALiCE (Almost Living Cell-free Expression) system, a lysate derived from tobacco cell suspension cultures that can be used to manufacture protein products for molecular and biochemical analysis as well as applications in the pharmaceutical industry.

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Conference papers on the topic "Recombinant protein"

Okafor, Paul, Zahed Siddique, and Talayeh Razzaghi. "Monitoring Recombinant Protein Titer in Escherichia Coli Fermentations Using Filtering Techniques." In 2024 IEEE International Conference on Big Data (BigData). IEEE, 2024. https://doi.org/10.1109/bigdata62323.2024.10825943.

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Patiño-Jurado, Brayan, Arturo Gaviria-Calderón, Manuel S. Moncada-Barrera, et al. "A Rapid Method for Ag85B Detection of Tuberculosis Using Label-Free Biosensor Based on an E-SMS Optical Fiber Structure." In Latin America Optics and Photonics Conference. Optica Publishing Group, 2024. https://doi.org/10.1364/laop.2024.w2a.2.

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In this work, etched singlemode-multimode-singlemode (E-SMS) optical fiber structures are evaluated as a biosensor through the binding between the immobilized recombinant Ag85B antigen and anti-Ag85B antibody. By tracking the wavelength response, it is demonstrated that the E-SMS devices can detect and measure low concentrations of anti-Ag85B in PBS solutions. This sensitive label-free biosensing technology for Ag85B protein detection has the potential to be applied for the detection of Mycobacterium tuberculosis and its evolution in clinical diagnosis as an alternative to the standard methods.

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Berkner, K. L., S. J. Busby, J. Gambee, and A. Kumar. "EXPRESSION IN MAMMALIAN CELLS OF FUSION PROTEINS BETWEEN HUMAN FACTORS IX AND VII." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643568.

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The vitamin K-dependent plasma proteins demonstrate remarkable similarities in their structures: all have multiple domains in common and extensive homology is observed within many of these domains. In order to investigate the structure-function relationship of these proteins, we have interchanged domains of one protein (factor IX) with that of another (factor VII) and have compared the expression of these fusion proteins with recombinant and native factors IX and VII. Oligonucleotide-directed mutagenesis was used to generate four fusion proteins: factor IX/VII-1, which contains the factor IX leader and gla domain fused to the growth factor and serine protease of factor VII; factor VII/IX-1, a reciprocal fusion protein of factor IX/VII-1; factor IX/VII-2, which contains the factor IX leader adjoined to the mature factor VII protein sequence; and factor VII/IX-2, the reciprocal fusion protein of factor IX/VII-2. The cDNAs encoding all four proteins were cloned into mammalian expression vectors, and to date three of these (factors IX/VII-1, 2 and VII/IX-1) have been transfected into baby hamster kidney (BHK) cells or 293 cells and characterized. Factors IX/VII-1 and VII/IX-1 were both secreted at levels comparable to recombinant factors IX and VII. The factor IX/VII-1 was identical in molecular weight to native or recombinant factor VII (i.e., 53 K). Factor VII/IX-1 was expressed as two proteins with molecular weights around 68 kd, as observed with recombinant factor IX. The factor IX/VII-1 protein has been purified to homogeneity and has been found to possess factor VII biological activity, but at a specific activity approximately 20% that of plasma factor VII. Thus, the gla domain of one clotting factor is capable of directing the activation of another and of generating biologically active protein. In contrast, no activity was observed with the factor IX/VII-2 fusion protein, indicating that there are limits to the interchanges which can generate functional blood clotting factors.

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Qiu, Weiguo, Arjun Stokes, Joseph Cappello, and Xiaoyi Wu. "Electrospinning of Recombinant Protein Polymer Nanofibers." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206352.

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Structural proteins often in the form of micro and nanofibers, constituting most of intra- and extracellular matrix (ECM), are the fundamental building blocks of life [1]. Recent efforts to replace diseased or damaged tissues and organs have resulted in the molecular design and genetic engineering of recombinant proteins, and the advent of new technology for fabricating structural proteins into micro-/nanofibrous scaffolds, hoping to resemble some or all the characteristics of ECM structure and function. The fabrication of such an ECM mimic may be an important step in engineering a functional tissue. To this end, we have produced a series of silk-elastin-like proteins (SELPs) [2]. Revealed by our subsequent studies, SELPs in the form of hydrogels, thin films, and microfibers, have displayed a set of outstanding biological and physical properties. In this study, electrospinning will be pursued as a mechanism for the formation of SELP nanofibers.

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Tyumentsev, A. I., M. A. Tyumentseva, and V. G. Akimkin. "DEVELOPMENT OF APPROACHES FOR ENDOTOXIN REMOVAL FROM PROTEIN PREPARATIONS ON THE EXAMPLE OF NUCLEASES OF THE CRISPR/CAS SYSTEM." In Molecular Diagnostics and Biosafety. Federal Budget Institute of Science 'Central Research Institute for Epidemiology', 2020. http://dx.doi.org/10.36233/978-5-9900432-9-9-113.

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Removal of bacterial endotoxins from solutions of recombinant proteins is one of the most important issues in the preparation of highly purified preparations suitable for in vivo use. An optimal technology for obtaining preparations purified from bacterial endotoxins has been proposed using purification of preparations of recombinant nucleases of the CRISPR/CAS system as an example. Efficacy of developed technology was compared with other available methods. Removal of bacterial endotoxins was carried out using Triton X-114 detergent added to a concentration of 1% to a solution containing the recombinant protein. It was shown that the content of bacterial endotoxins in solutions of purified proteins obtained according to the proposed technology is 0.3–1.5 EU/ml.

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Qiu, Weiguo, Yiding Huang, Joseph Cappello, and Xiaoyi Wu. "Electrospun Recombinant Protein Polymer Nanofibers as a Biomaterial." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13131.

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Micro/nanometer protein fibers are fundamental building blocks of extra-/intracellular matrices, providing structural support, stability and protection to cells, tissue and organism [1]. Fabricating performance protein micro/nanofibers has been extensively pursued for a variety of biomedical application. In this study, silk-elastinlike protein (SELP) polymer will be electrospun into nanofibers as a biomaterial.

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Teng, Weibing, Yiding Huang, Joseph Cappello, and Xiaoyi Wu. "Mechanical and In-Vitro Cell Compatibility Properties of Silk-Elastinlike Protein-Based Biomaterial." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13141.

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A series of genetically engineered recombinant silk-elastinlike proteins (SELPs) have been produced by combining polypeptide sequences derived from native silk of superior mechanical strength and elastin that is extremely durable and resilient. They have displayed a set of outstanding properties such as good biocompatibility and controllable biodegradation rates. In the study, we characterized the mechanical property of genetically engineered, recombinant silk-elastinlike protein copolymer, SELP-47K, under physical and chemical treatments. The biocompatibility of the SELP-47K was also evaluated by cell culture. The ultimate goal of this study is to explore the potential of SELPs for applications in the engineering of load-bearing tissues such as arteries.

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Tsmokalyuk, D. A., A. A. Zagorskaya, P. A. Belavin, E. A. Uvarova, and E. V. Deineko. "IDENTIFICATION OF TRANSGENE INTEGRATION REGIONS IN THE ARABIDOPSIS THALIANA GENOME, PROVIDING A HIGH YIELD OF THE RECOMBINANT PROTEIN." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-143.

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This work summarizes the results of genomic safe harbor method implementation for increasing recombinant protein yield in the transgenic plants. A collection of transgenic Arabidopsis thaliana plants was assessed for recombinant protein accumulation level. For plants with superior accumulation level (up to 0,8 % of total soluble protein) adjacent to transgene genomic sequences were defined.

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Shetty, R. S., Lyndon L. Salins, S. Ramanathan, and Sylvia Daunert. "Recombinant methods in protein and whole-cell biosensing." In Photonics East '99, edited by Mahmoud Fallahi and Basil I. Swanson. SPIE, 1999. http://dx.doi.org/10.1117/12.372904.

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Neklesova, M. V., and N. Deeb. "PRODUCTION OF RECOMBINANT PROTEINS AMUC_1100 AND P9 AND ASSESSMENT OF THEIR IN VITRO ANTITUMOR ACTIVITY." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-106.

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The probiotic properties of Akkermansia muciniphila in the treatment of metabolic, cardiovascular and oncological diseases are mediated by the surface protein Amuc_1100 (Amuc) and secreted protein P9, but their combined effect has not been investigated. In this work, a recombinant producer E. coli BL21(DE3) of proteins Amuc and P9 was obtained. It is planned to conduct experiments on the colorectal cancer cell line using a combination of Amuc and P9.

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Reports on the topic "Recombinant protein"

Veen, Ryan Vander, Mark Mogler, Matthew M. Erdman, and D. L. Hank Harris. Preparation of GP5-M Heterodimer Glycantype Specific Recombinant Protein and Replicon Particles. Iowa State University, 2009. http://dx.doi.org/10.31274/ans_air-180814-698.

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Walls, Lichun H. Isolation and Preliminary Characterization of a Recombinant TAT Protein From Human Immunodeficiency Virus. Defense Technical Information Center, 1995. http://dx.doi.org/10.21236/ada298304.

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นุชประยูร, อิศรางค์. การศึกษาโปรตีนที่สำคัญในพิษงูแมวเซาเพื่อนำมาดัดแปลงใช้ประโยชน์ทางการแพทย์ : รายงานการวิจัยฉบับสมบูรณ์. จุฬาลงกรณ์มหาวิทยาลัย, 2008. https://doi.org/10.58837/chula.res.2008.26.

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ปัญหางูพิษกัดเป็นปัญหาทางสาธารณสุขที่สำคัญของประเทศไทย หนึ่งในงูพิษที่สำคัญในไทยคือ งูแมวเซา (Daboia russellii siamensis) งูชนิดนี้พบมากในแถบภาคกลางและภาคตะวันออกของไทย ผู้ที่ถูกงูชนิดนี้กัด มักมีอาการทางระบบเลือด และภาวะไตวายเฉียบพลัน ซึ่งเป็นสาเหตุสำคัญที่ทำให้ผู้ที่ถูกงูแมวเซากัดเสียชีวิต ในปัจจุบันความรู้เกี่ยวกับกลไกการเกิดพิษหลังถูกงูแมวเซากัด รวมทั้งโปรตีนสำคัญในพิษงูแมวเซาที่อาจมีประโยชน์ทางการแพทย์ ยังไม่มีการศึกษาอย่างแน่ชัด การศึกษาองค์ประกอบของพิษงูแมวเซาในเชิงลึก จะช่วยให้เข้าใจกลไกการเกิดพิษ นำไปสู่การรักษาที่มีประสิทธิภาพที่ดีขึ้น พร้อมทั้งอาจนำความรู้ที่ได้ไปใช้ประโยชน์ในทางการแพทย์ต่อไป จากผลงานที่ผ่านมา ทางกลุ่มผู้วิจัยได้สร้างห้องสมุดยีน (cDNA library) จากต่อมพิษงูแมวเซาได้สำเร็จ และได้มีการศึกษาองค์ประกอบของพิษงูเบื้องต้นด้วยเทคนิค Expressed Sequence Tags Analysis พบว่าในพิษงูมีการแสดงออกของยีนที่เกี่ยวข้องกับกระบวนการ haematostasis เป็นจำนวนมาก ซึ่งสัมพันธ์กับความเป็นพิษของงูแมวเซาที่มีผลโดยตรงต่อระบบเลือดของเหยื่อที่ถูกกัด โปรตีนที่พบมากคือ phospholipase A2, faetor X activating enzyme (RVV-X), factor V activating enzyme (RVV-V) และโปรตีนอื่นๆ อีกหลายชนิด จากการทบทวนวรรณกรรม โปรตีนพิษงูแมวเซาที่น่าสนใจคือ RVV-X และ PLA2 ดังนั้นในการศึกษานี้จึงได้แยกโปรตีนพิษงูชนิด RVV-X และ PLA2 จากพิษงูแมวเซาของไทยก่อน โดยใช้วิธี Gel filtration column Chromatography และ Anion exchange column chromatography จากนั้นยืนยันผลการแยกบริสุทธิ์โปรตีนพิษงูชนิด RVV-X และ PLA2 และหาขนาดของโปรตีนพิษงูทั้ง 2 ชนิด โดยใช้วิธี MALDI-TOF mass spectrometry พบว่าโปรตีนพิษงูแมวเซาทั้งชนิด RVV-X และ PLA2 มีความบริสุทธิ์สูงและมีขนาดโปรตีนประมาณ 90 และ 14 Kb ใน non-reducing condition ตามลำดับ จากนั้นได้ทดสอบคุณสมบัติทางชีวเคมีของ RVV-X และ PLA2 ที่แยกบริสุทธิ์ได้ พบว่าโปรตีนทั้งสองชนิดมี enzymatic activity สูง โครงการนี้เป็นโครงการวิจัยต่อเนื่อง 3 ปี (พ.ศ. 2550-2552) ซึ่งในขณะนี้อยู่ในระหว่างการโคลนยีนต่างๆ ที่สำคัญในพิษงูแมวเซาไทยจากห้องสมุดยีน และทำการ express ยีนเหล่านี้เพื่อสร้าง recombinant proteins ที่คาดว่าจะมีความสามารถในการทำงานได้เหมือน native protein รวมทั้งศึกษาโปรตีนชนิดต่างๆ ในพิษงูที่ได้จากทั้งวิธีแยกโปรตีนในพิษงูโดยเทคนิคทางชีวเคมี หรือจาก recombinant proteins เพื่อหาโปรตีนเป้าหมายที่สำคัญต่อการกลไกการเกิดพิษหลังถูกงูแมวเซากัด และอาจนำความรู้ที่ได้ไปใช้ประโยชน์ในทางการแพทย์ต่อไป

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Galili, Gad, and Alan Bennett. Role of Molecular Chaperone in Wheat Storage Protein Assembly. United States Department of Agriculture, 1995. http://dx.doi.org/10.32747/1995.7604926.bard.

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Following sequestration into the ER, wheat gliadins assemble into complexes that initiate the formation of protein bodies. In the present work we have characterized the DNA sequence and regulation of expression of a plant BiP and also studied its interaction with wheat storage proteins as well as its role in the maturation of these storage proteins. In the Israeli lab, immunoprecipitation studies were made using anti BiP and anti storage proteins sera, both in wheat and in transgenic tobacco plants expressing a wheat gliadin storage proteins. In both cases, we could show that BiP interacts with the gliadin storage proteins. In addition, we could show that BiP also played an important role in the initial assembly of the gliadins. In the American lab, the complexity, structure and properties of tomato BiP was characterized at the molecular and biochemical levels. In addition, tomato BiP was also overexpressed in bacteria and the overexpressed protein was found to be active. The cooperative findings of the Israeli and American labs clearly improves our understanding of the structure and expression of a plant BiP as well as its role in the maturation of storage proteins in plants seeds. In addition, it will serve as a foundation for future studies of the mechanisms of BiP function in in vitro studies using purified storage proteins and purified recombinant active BiP.

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นุชประยูร, อิศรางค์, มณฑน์มาศ สุนทราวัฒน์ та ธัญณิชา อ่อนดี. การศึกษาโปรตีน ที่สำคัญในพิษงูแมวเซาเพื่อนำมาดัดแปลงใช้ประโยชน์ทางการแพทย์ : รายงานการวิจัยฉบับสมบูรณ์. จุฬาลงกรณ์มหาวิทยาลัย, 2009. https://doi.org/10.58837/chula.res.2009.23.

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ปัญหางูพิษกัดเป็นปัญหาทางสาธารณะสุขที่สำคัญของประเทศไทย หนึ่งในงูพิษที่สำคัญในไทยคืองูแมวเซา (Daboia russellii siamensis) งูชนิดนี้พบมากในแถบภาคกลางและภาคตะวันออกของไทย ผู้ที่ถูกงูชนิดนี้กัด มักมีอาการทางระบบเลือด และภาวะไตวายเฉียบพลัน ซึ่งเป็นสาเหตุสำคัญที่ทำให้ผู้ที่ถูกงูแมวเซากัดเสียชีวิต ในปัจจุบันความรู้เกี่ยวกับกลไกการเกิดพิษหลังถูกงูแมวเซากัด รวมทั้งโปรตีนสำคัญในพิษงูแมวเซาที่อาจมีประโยชน์ทางการแพทย์ ยังไม่มีการศึกษาอย่างแน่ชัด การศึกษาองค์ประกอบของพิษงูแมวเซาในเชิงลึก จะช่วยให้เข้าใจกลไกการเกิดพิษ นำไปสู่การรักษาที่มีประสิทธิภาพที่ดีขึ้น พร้อมทั้งอาจนำความรู้ที่ได้ไปใช้ประโยชน์ในทางการแพทย์ต่อไป จากผลงานที่ผ่านมา ทางกลุ่มผู้วิจัยได้สร้างห้องสมุดยีน (cDNA library) จากต่อมพิษงูแมวเซาได้สำเร็จ และได้มีการศึกษาองค์ประกอบของพิษงูเบื้องต้นด้วยเทคนิค Expressed Sequence Tags Analysis พบว่าในพิษงูมีการแสดงออกของยีนที่เกี่ยวข้องกับกระบวนการ haematostasis เป็นจำนวนมาก ซึ่งสัมพันธ์กับความเป็นพิษของงูแมวเซาที่มีผลโดยตรงต่อระบบเลือดของเหยื่อที่ถูกกัด หลังจากการศึกษาวิจัยในปีแรกได้ทำการแยกบริสุทธิ์โปรตีนพิษงูแมวเซาชนิด RVV-X และ PLA2 ก่อนโดยใช้วิธี Gel filtration column chromatography และ Anion exchange column chromatography และทำโคลนและผลิตโปรตีนที่พบใน cDNA library ด้วย recombinant technology จำนวน 5 ยีน ได้สำเร็จ คือ phospholipase A2 (PLA2), factor X activating enzyme (RVV-X), factor V activating enzyme (RVV-V), serine β-fibrinogenase และ rJerdostatin homolog (Daboistatin short disintegrin) โดยที่โปรตีนทุกตัวสามารถทำปฏิกิริยากับ anti his tag ได้ โดยในการศึกษานี้เป็นการทดสอบคุณสมบัติทางชีวเคมีของโปรตีน RVV-X ทั้งในหลอดทดลองและในสัตว์ทดลอง รวมถึงการทดสอบการทำงานของ recombinant protein ที่ผลิตได้ ซึ่งสามารถนำความรู้ที่ได้ไปใช้ประโยชน์ในทางการแพทย์ต่อไป

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Banai, Menachem, and Gary Splitter. Molecular Characterization and Function of Brucella Immunodominant Proteins. United States Department of Agriculture, 1993. http://dx.doi.org/10.32747/1993.7568100.bard.

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The BARD project was a continuation of a previous BARD funded research project. It was aimed at characterization of the 12kDa immunodominant protein and subsequently the cloning and expression of the gene in E. coli. Additional immunodominant proteins were sought among genomic B. abortus expression library clones using T-lymphocyte proliferation assay as a screening method. The 12kDa protein was identified as the L7/L12 ribosomal protein demonstrating in the first time the role a structural protein may play in the development of the host's immunity against the organism. The gene was cloned from B. abortus (USA) and B. melitensis (Israel) showing identity of the oligonucleotide sequence between the two species. Further subcloning allowed expression of the protein in E. coli. While the native protein was shown to have DTH antigenicity its recombinant analog lacked this activity. In contrast the two proteins elicited lymphocyte proliferation in experimental murine brucellosis. CD4+ cells of the Th1 subset predominantly responded to this protein demonstrating the development of protective immunity (g-IFN, and IL-2) in the host. Similar results were obtained with bovine Brucella primed lymphocytes. UvrA, GroE1 and GroEs were additional Brucella immunodominant proteins that demonstrated MHC class II antigenicity. The role cytotoxic cells are playing in the clearance of brucella cells was shown using knock out mice defective either in their CD4+ or CD8+ cells. CD4+ defective mice were able to clear brucella as fast as did normal mice. In contrast mice which were defective in their CD8+ cells could not clear the organisms effectively proving the importance of this subtype cell line in development of protective immunity. The understanding of the host's immune response and the expansion of the panel of Brucella immunodominant proteins opened new avenues in vaccine design. It is now feasible to selectively use immunodominant proteins either as subunit vaccine to fortify immunity of older animals or as diagnostic reagents for the serological survaillance.

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Palmer, Guy H., Eugene Pipano, Terry F. McElwain, Varda Shkap, and Donald P. Knowles, Jr. Development of a Multivalent ISCOM Vaccine against Anaplasmosis. United States Department of Agriculture, 1993. http://dx.doi.org/10.32747/1993.7568763.bard.

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Anaplasmosis is an arthropod+borne disease of cattle caused by the rickettsia Anaplasma marginale and an impediment to efficient production of healthy livestock in both Israel and the United States. Our research focuses on development of a recombinant membrane surface protein (MSP) immunogen to replace current vaccines derived from the blood of infected cattle. The risk of widespread transmission of both known and newly emergent pathogens has prevented licensure of live blood-based vaccines in the U.S. and is a major concern for their continued use in Israel. Briefly, we accomplished the following in our BARD supported research: i) characterization of the intramolecular and intermolecular relationships of the native Major Surface Proteins (MSP) in the outer membrane; ii) expression, purification, and epitope characterization of the recombinant MSP-2, MSP-3, MSP-4, and MSP-5 proteins required to construct the recombinant ISCOM; iii) demonstration that the outer membrane-Quil A induces CD4+ T lymphocytes specific for the outer membrane polypeptides; iv) identification of CD4+ T lymphocytes that recognize outer membrane polypeptide epitopes conserved among other wise antigenically distinct strains; v) determination that immunization with the outer membrane-Quil A construct does not affect the ability of ticks to acquire or transmit A. marginale; and vi) demonstration that the outer membrane-Quil A construct induces complete protection against rickettsemia upon homologous challenge and significant protection against challenge with antigenically distinct strains, including tick transmission. Importantly, the level of protection against homologous challenge in the MSP vaccinates was comparable to that induced by live blood-based vaccines and demonstrates that development of a new generation of vaccines is feasible.

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Bercovier, Herve, Raul Barletta, and Shlomo Sela. Characterization and Immunogenicity of Mycobacterium paratuberculosis Secreted and Cellular Proteins. United States Department of Agriculture, 1996. http://dx.doi.org/10.32747/1996.7573078.bard.

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Our long-term goal is to develop an efficient acellular vaccine against paratuberculosis based on protein antigen(s). A prerequisite to achieve this goal is to analyze and characterize Mycobacterium paratuberculosis (Mpt) secreted and cellular proteins eliciting a protective immune response. In the context of this general objective, we proposed to identify, clone, produce, and characterize: the Mpt 85B antigen and other Mpt immunoreactive secreted proteins, the Mpt L7/L12 ribosomal protein and other immunoreactive cellular proteins, Mpt protein determinants involved in invasion of epithelial cells, and Mpt protein antigens specifically expressed in macrophages. Paratuberculosis is still a very serious problem in Israel and in the USA. In the USA, a recent survey evaluated that 21.6% of the dairy herd were infected with Mpt resulting in 200-250 million dollars in annual losses. Very little is known on the virulence factors and on protective antigens of Mpt. At present, the only means of controlling this disease are culling or vaccination. The current vaccines do not allow a clear differentiation between infected and vaccinated animals. Our long-term goal is to develop an efficient acellular paratuberculosis vaccine based on Mpt protein antigen(s) compatible with diagnostic tests. To achieve this goal it is necessary to analyze and characterize secreted and cellular proteins candidate for such a vaccine. Representative Mpt libraries (shuttle plasmid and phage) were constructed and used to study Mpt genes and gene products described below and will be made available to other research groups. In addition, two approaches were performed which did not yield the expected results. Mav or Mpt DNA genes that confer upon Msg or E. coli the ability to invade and/or survive within HEp-2 cells were not identified. Likewise, we were unable to characterize the 34-39 kDa induced secreted proteins induced by stress factors due to technical difficulties inherent to the complexity of the media needed to support substantial M. pt growth. We identified, isolated, sequenced five Mpt proteins and expressed four of them as recombinant proteins that allowed the study of their immunological properties in sensitized mice. The AphC protein, found to be up regulated by low iron environment, and the SOD protein are both involved in protecting mycobacteria against damage and killing by reactive oxygen (Sod) and nitrogen (AhpC) intermediates, the main bactericidal mechanisms of phagocytic cells. SOD and L7/L12 ribosomal proteins are structural proteins constitutively expressed. 85B and CFP20 are both secreted proteins. SOD, L7/L12, 85B and CFP20 were shown to induce a Th1 response in immunized mice whereas AphC was shown by others to have a similar activity. These proteins did not interfere with the DTH reaction of naturally infected cows. Cellular immunity provides protection in mycobacterial infections, therefore molecules inducing cellular immunity and preferentially a Th1 pathway will be the best candidate for the development of an acellular vaccine. The proteins characterized in this grant that induce a cell-mediated immunity and seem compatible with diagnostic tests, are good candidates for the construction of a future acellular vaccine.

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Chan, Eva. Expression and Purification of Recombinant Protein to Generate a Monoclonal Antibody to the PX domain of Tks5 ? Isoform in Cancer Cells. Portland State University Library, 2016. http://dx.doi.org/10.15760/honors.323.

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Angov, Evelina. Production of a Recombinant E. coli Expressed Malarial Vaccine from the C-Terminal Fragment of Plasmodium Falciparum 3D7 Merozoite Surface Protein-1. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada391249.

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