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Letteratura scientifica selezionata sul tema "Escherichia coli Inclusions"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 1 febbraio 2022

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Articoli di riviste sul tema "Escherichia coli Inclusions"

Hänisch, Jan, Marc Wältermann, Horst Robenek, and Alexander Steinbüchel. "The Ralstonia eutropha H16 phasin PhaP1 is targeted to intracellular triacylglycerol inclusions in Rhodococcus opacus PD630 and Mycobacterium smegmatis mc2155, and provides an anchor to target other proteins." Microbiology 152, no. 11 (November 1, 2006): 3271–80. http://dx.doi.org/10.1099/mic.0.28969-0.

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In Ralstonia eutropha, the H16 phasin PhaP1 represents the major phasin that binds to the surface of polyhydroxyalkanoate (PHA) inclusions. In this study, C-terminal fusions of PhaP1 with enhanced green fluorescent protein (eGFP) and with Escherichia coli β-galactosidase (LacZ) were expressed separately in the triacylglycerol (TAG)-accumulating actinomycetes Rhodococcus opacus PD630 and Mycobacterium smegmatis mc2155, employing the M. smegmatis acetamidase (ace) promoter of the Escherichia–Mycobacterium/Rhodococcus shuttle plasmid pJAM2. PhaP1 and the PhaP1 fusion proteins were expressed stably in the recombinant strains. Western blot analysis of cell fractions of Rh. opacus revealed that PhaP1 and the PhaP1–eGFP fusion protein were associated with the TAG inclusions, whereas no phasin or phasin fusion protein was detected in the soluble and membrane fractions. Additional electron microscopy/immunocytochemistry studies demonstrated that PhaP1 was mainly located on the surface of intracellular TAG inclusions; in addition, some PhaP1 also occurred at the plasma membrane. Fluorescence microscopic investigations of the subcellular distribution of the PhaP1–eGFP fusion protein in vivo and on isolated TAG inclusions revealed that the fusion protein was bound to TAG inclusions at all stages of their formation, and to some extent at the cytoplasmic membrane. The PhaP1–LacZ fusion protein also bound to the TAG inclusions, and could be separated together with the inclusions from Rh. opacus crude extracts, thus demonstrating the immobilization of β-galactosidase activity on the inclusions. This is believed to be the first report demonstrating the ability of PhaP1 to bind to lipid inclusions in addition to PHA inclusions. Furthermore, it was demonstrated that this non-specificity of PhaP1 can be utilized to anchor enzymically active fusion proteins to a matrix of bacterial TAG inclusions.

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Chen, Shuxiong, Natalie A. Parlane, Jason Lee, D. Neil Wedlock, Bryce M. Buddle, and Bernd H. A. Rehm. "New Skin Test for Detection of Bovine Tuberculosis on the Basis of Antigen-Displaying Polyester Inclusions Produced by Recombinant Escherichia coli." Applied and Environmental Microbiology 80, no. 8 (February 14, 2014): 2526–35. http://dx.doi.org/10.1128/aem.04168-13.

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ABSTRACTThe tuberculin skin test for diagnosing tuberculosis (TB) in cattle lacks specificity if animals are sensitized to environmental mycobacteria, as some antigens in purified protein derivative (PPD) prepared fromMycobacterium bovisare present in nonpathogenic mycobacteria. Three immunodominant TB antigens, ESAT6, CFP10, and Rv3615c, are present in members of the pathogenicMycobacterium tuberculosiscomplex but absent from the majority of environmental mycobacteria. These TB antigens have the potential to enhance skin test specificity. To increase their immunogenicity, these antigens were displayed on polyester beads by translationally fusing them to a polyhydroxyalkanoate (PHA) synthase which mediated formation of antigen-displaying inclusions in recombinantEscherichia coli. The most common form of these inclusions is poly(3-hydroxybutyric acid) (PHB). The respective fusion proteins displayed on these PHB inclusions (beads) were identified using tryptic peptide fingerprinting analysis in combination with matrix-assisted laser desorption ionization–time of flight mass spectrometry (MALDI-TOF MS). The surface exposure and accessibility of antigens were assessed by enzyme-linked immunosorbent assay (ELISA). Polyester beads displaying all three TB antigens showed greater reactivity with TB antigen-specific antibody than did beads displaying only one TB antigen. This was neither due to cross-reactivity of antibodies with the other two antigens nor due to differences in protein expression levels between beads displaying single or three TB antigens. The triple-antigen-displaying polyester beads were used for skin testing of cattle and detected all cattle experimentally infected withM. boviswith no false-positive reactions observed in those sensitized to environmental mycobacteria. The results suggested applicability of TB antigen-displaying polyester inclusions as diagnostic reagents for distinguishing TB-infected from noninfected animals.

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Davis, Katelin L., Liang Cheng, José Ramos-Vara, Melissa D. Sánchez, Rebecca P. Wilkes, and Mario F. Sola. "Malakoplakia in the Urinary Bladder of 4 Puppies." Veterinary Pathology 58, no. 4 (April 23, 2021): 699–704. http://dx.doi.org/10.1177/03009858211009779.

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Malakoplakia in humans most often affects the urinary bladder and is characterized by inflammation with von Hansemann–type macrophages, with or without Michaelis-Gutmann bodies, and is frequently associated with Escherichia coli infection. We describe the microscopic features of malakoplakia in the urinary bladder of 4 puppies. In all cases, the lamina propria of the urinary bladder was markedly expanded by sheets of large, round to polygonal macrophages with intracytoplasmic, periodic acid-Schiff-positive granules and granular inclusions, and rare Prussian blue–positive inclusions. Macrophages were positive for CD18 and Iba1. In 2 cases, Michaelis-Gutmann bodies were detected with hematoxylin and eosin stain and were best demonstrated with von Kossa stain. E. coli infection was confirmed in 2 cases with bacterial culture or polymerase chain reaction (PCR) and sequencing of the bacterial 16S ribosomal RNA gene. Transmission electron microscopy of one case demonstrated macrophages with abundant lysosomes, phagolysosomes, and rod-shaped bacteria. Microscopic features were similar to human cases of malakoplakia. In dogs, the light microscopic characteristics of malakoplakia closely resemble granular cell tumors and histiocytic ulcerative colitis.

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Wada, Y., H. Kondo, Y. Nakaoka, and M. Kubo. "Gastric Attaching and Effacing Escherichia coli Lesions in a Puppy with Naturally Occurring Enteric Colibacillosis and Concurrent Canine Distemper Virus Infection." Veterinary Pathology 33, no. 6 (November 1996): 717–20. http://dx.doi.org/10.1177/030098589603300615.

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A puppy suffering from chronic diarrhea was humanely killed at 90 days of age. Numerous Gram-negative bacilli were found adhering to the surface of as well as within epithelial cells from the stomach to the colon. Canine distemper virus inclusions were in the epithelial cytoplasm of the esophageal, gastric, and intestinal mucosa. Typical attaching and effacing ultrastructural lesions were in the stomach, and some bacilli were in the cytoplasm of the epithelial cells, Escherichia coli, isolated from the contents of the small intestine, belonged to serotype 0118: NM and were negative for plasmid-encoded EPEC adherence factor (EAF) and positive for the E. coli attaching effacing ( eae) gene. Immunohistologically, bacilli attached to the epithelium from the stomach to the colon were positive for antisera against E. coli 0118. E. coli0118: NM inoculated into human tissue culture cells (HEp-2 cells) were attached to the surface of the cells and within the cytoplasm. This is the first report of attaching and effacing E. coli (AEEC) infection in the stomach of the dog.

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Aldrich, H. C., S. Elvington, HE Machines, R. Szabady, K. Feder, L. McDowell, and J. M. Shively. "Ultrastructural and Cytochemical Analyses of the Expression of the Thiobacillus Carboxysome Operon in Escherichia Coli." Microscopy and Microanalysis 7, S2 (August 2001): 740–41. http://dx.doi.org/10.1017/s1431927600029779.

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The cytoplasm of the bacterium Thiobacillus neapolitanus contains 117 nm diameter polyhedral inclusions, “carboxysomes” (Fig. 1) that contain ribulose-1,5- bisphosphate carboxylase/oxygenase (RuBisCO). Surrounding the polyhedron are nonmembranous proteinaceous plates devoid of lipid. The carboxysomes are composed of at least 8 major peptides, all coded within the same operon. Six (CsoSIA, CsoSIB, CsoSIC, CsoS2A, CsoS2B, and CsoS3) make up the shell, and two are the large (CbbL) and small subunits (CbbS) of RuBisCO. Using immunogold labeling on ultrathin sections, peptides CsoS2A, CsoS2B, and CsoS3 have been localized to the shell. Since the original characterization of the csoSl gene, we have also immunolocalized the CsoSl peptide to the shell.As part of our initial efforts to understand how these components are assembled into the symmetrical, functional entity, the carboxysome operon from T. neapolitanus was cloned into the pET-21a(+) plasmid, an expression vector that codes for resistance to ampicillin.

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Blatchford, Paul A., Colin Scott, Nigel French, and Bernd H. A. Rehm. "Immobilization of organophosphohydrolase OpdA from Agrobacterium radiobacter by overproduction at the surface of polyester inclusions inside engineered Escherichia coli." Biotechnology and Bioengineering 109, no. 5 (December 26, 2011): 1101–8. http://dx.doi.org/10.1002/bit.24402.

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Kalscheuer, Rainer, Tim Stöveken, Heinrich Luftmann, Ursula Malkus, Rudolf Reichelt, and Alexander Steinbüchel. "Neutral Lipid Biosynthesis in Engineered Escherichia coli: Jojoba Oil-Like Wax Esters and Fatty Acid Butyl Esters." Applied and Environmental Microbiology 72, no. 2 (February 2006): 1373–79. http://dx.doi.org/10.1128/aem.72.2.1373-1379.2006.

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ABSTRACT Wax esters are esters of long-chain fatty acids and long-chain fatty alcohols which are of considerable commercial importance and are produced on a scale of 3 million tons per year. The oil from the jojoba plant (Simmondsia chinensis) is the main biological source of wax esters. Although it has a multitude of potential applications, the use of jojoba oil is restricted, due to its high price. In this study, we describe the establishment of heterologous wax ester biosynthesis in a recombinant Escherichia coli strain by coexpression of a fatty alcohol-producing bifunctional acyl-coenzyme A reductase from the jojoba plant and a bacterial wax ester synthase from Acinetobacter baylyi strain ADP1, catalyzing the esterification of fatty alcohols and coenzyme A thioesters of fatty acids. In the presence of oleate, jojoba oil-like wax esters such as palmityl oleate, palmityl palmitoleate, and oleyl oleate were produced, amounting to up to ca. 1% of the cellular dry weight. In addition to wax esters, fatty acid butyl esters were unexpectedly observed in the presence of oleate. The latter could be attributed to solvent residues of 1-butanol present in the medium component, Bacto tryptone. Neutral lipids produced in recombinant E. coli were accumulated as intracytoplasmic inclusions, demonstrating that the formation and structural integrity of bacterial lipid bodies do not require specific structural proteins. This is the first report on substantial biosynthesis and accumulation of neutral lipids in E. coli, which might open new perspectives for the biotechnological production of cheap jojoba oil equivalents from inexpensive resources employing recombinant microorganisms.

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Petrus, Marloes L. C., Lukas A. Kiefer, Pranav Puri, Evert Heemskerk, Michael S. Seaman, Dan H. Barouch, Sagrario Arias, Gilles P. van Wezel, and Menzo Havenga. "A microbial expression system for high-level production of scFv HIV-neutralizing antibody fragments in Escherichia coli." Applied Microbiology and Biotechnology 103, no. 21-22 (October 22, 2019): 8875–88. http://dx.doi.org/10.1007/s00253-019-10145-1.

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Abstract Monoclonal antibodies (mABs) are of great biopharmaceutical importance for the diagnosis and treatment of diseases. However, their production in mammalian expression hosts usually requires extensive production times and is expensive. Escherichia coli has become a new platform for production of functional small antibody fragment variants. In this study, we have used a rhamnose-inducible expression system that allows precise control of protein expression levels. The system was first evaluated for the cytoplasmic production of super folder green fluorescence protein (sfGFP) in various production platforms and then for the periplasmic production of the anti-HIV single-chain variable antibody fragment (scFv) of PGT135. Anti-HIV broadly neutralizing antibodies, like PGT135, have potential for clinical use to prevent HIV transmission, to promote immune responses and to eradicate infected cells. Different concentrations of L-rhamnose resulted in the controlled production of both sfGFP and scFv PGT135 antibody. In addition, by optimizing the culture conditions, the amount of scFv PGT135 antibody that was expressed soluble or as inclusions bodies could be modulated. The proteins were produced in batch bioreactors, with yields of 4.9 g/L for sfGFP and 0.8 g/L for scFv. The functionality of the purified antibodies was demonstrated by their ability to neutralize a panel of different HIV variants in vitro. We expect that this expression system will prove very useful for the development of a more cost-effective production process for proteins and antibody fragments in microbial cells.

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Carija, Pinheiro, Iglesias, and Ventura. "Computational Assessment of Bacterial Protein Structures Indicates a Selection Against Aggregation." Cells 8, no. 8 (August 8, 2019): 856. http://dx.doi.org/10.3390/cells8080856.

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The aggregation of proteins compromises cell fitness, either because it titrates functional proteins into non-productive inclusions or because it results in the formation of toxic assemblies. Accordingly, computational proteome-wide analyses suggest that prevention of aggregation upon misfolding plays a key role in sequence evolution. Most proteins spend their lifetimes in a folded state; therefore, it is conceivable that, in addition to sequences, protein structures would have also evolved to minimize the risk of aggregation in their natural environments. By exploiting the AGGRESCAN3D structure-based approach to predict the aggregation propensity of >600 Escherichia coli proteins, we show that the structural aggregation propensity of globular proteins is connected with their abundance, length, essentiality, subcellular location and quaternary structure. These data suggest that the avoidance of protein aggregation has contributed to shape the structural properties of proteins in bacterial cells.

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Rybalchenko, O. V., O. G. Orlova, L. B. Zakharova, O. N. Vishnevskaya, and A. G. Markov. "EFFECT OF PROBIOTIC BACTERIA AND LIPOPOLISACCHARIDES ON EPITELIOCYTES TIGHT JUNCTIONS OF RAT JEJUNUM." Journal of microbiology epidemiology immunobiology, no. 6 (December 28, 2017): 80–87. http://dx.doi.org/10.36233/0372-9311-2017-6-80-87.

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Aim. The present study has been undertaken with the main objective the influence of probiotic bacteria Lactobacillus plantarum 8 РАЗ and Escherichia coli M17 and lipopolysaccharide on the ultrastructure of enterocytes tight junctions of mucous membranes of rat jejunum. Materials and methods. The study was carried out on E. coli lipopolysaccharide (Sigma-Aldrich, Germany) and probiotic bacteria L. plantarum 8PA3 and E. coli M17. Male Wistar rats were used. A comparative analysis of the ultrathin structure of enterocytes and tight junctions were carried out by successive incubation of rat jejunum with probiotic bacteria L. plantarum 8PA3 and E. coli Ml 7, with lipopolysaccharide and a complex of bacteria with LPS. Results. The effect of L. plantarum 8PA3 on the mucosa of rats jejunum on a number of characters was similar to E. coli Mil. It manifested by preservation of the intact structure of the intercellular space and tight junctions. At the same time, hollow spherical inclusions with fragments of bacteria surrounded by membranes detected in the cytoplasm of enterocytes testified to the possibility of penetration of probiotic bacteria through the mucous membrane of the jejunum by a transcellular pathway With simultaneous action on enterocytes of rats jejunum of probiotic bacteria and lipopolysaccharide complex no destructive changes in the structure of dense contacts were observed, however, in a significant number of cases, bacterial cells were found in the intercellular space next to the goblet cells. Conclusion. A similar effect of Gram-positive bacteria L. plantarum 8PA3 and Gram-negative bacteria E. coli Ml 7 and their complexes with lipopolysaccharide on the jejunum epitheliocytes was revealed. Morphological analysis showed that lipopolysaccharide might influence on parasel-lular transport by probiotic bacteria. In the absence of LPS, probiotic bacteria can possibly penetrate the mucosa of rats jejunum by a transcellular pathway.

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Più fonti

Tesi sul tema "Escherichia coli Inclusions"

RODRIGUES, DANIELLA. "Utilização de altas pressões hidrostáticas para o estudo e renaturação de proteínas com estrutura quaternária." reponame:Repositório Institucional do IPEN, 2012. http://repositorio.ipen.br:8080/xmlui/handle/123456789/10161.

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Made available in DSpace on 2014-10-09T12:35:27Z (GMT). No. of bitstreams: 0 Made available in DSpace on 2014-10-09T14:06:25Z (GMT). No. of bitstreams: 0 Dissertação (Mestrado) IPEN/D Instituto de Pesquisas Energeticas e Nucleares - IPEN-CNEN/SP

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Wangsa-Wirawan, Norbertus Djajasantosa. "Physicochemical properties of protein inclusion bodies." Title page, contents and introduction only, 1999. http://web4.library.adelaide.edu.au/theses/09PH/09phw2465.pdf.

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Bibliography: leaves 182-198. Improvements in the current production system of inclusion bodies and the downstream processing sequence are essential to maintain a competitive advantage in the market place. Optimisation of fermentation is considered to improve production yield; then flotation as a possible inclusion body recovery method.

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BALDUINO, KELI N. "Renaturacao em altas pressoes hidrostaticas de proteinas recombinantes agregadas em corpos de inclusao produzidos em Eschirichia coli." reponame:Repositório Institucional do IPEN, 2009. http://repositorio.ipen.br:8080/xmlui/handle/123456789/9457.

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Made available in DSpace on 2014-10-09T12:26:58Z (GMT). No. of bitstreams: 0 Made available in DSpace on 2014-10-09T14:03:47Z (GMT). No. of bitstreams: 0 Dissertacao (Mestrado) IPEN/D Instituto de Pesquisas Energeticas e Nucleares - IPEN-CNEN/SP

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Wong, Heng Ho. "Modelling studies of the interaction between homogenisation, centrifugation and inclusion body dissolution /." Title page, contents and summary only, 1997. http://web4.library.adelaide.edu.au/theses/09PH/09phw8718.pdf.

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Saulou, Claire. "Evaluation des propriétés anti-adhésives et biocides de films nanocomposites avec inclusions d’argent, déposés sur acier inoxydable par procédé plasma." Toulouse, INSA, 2009. http://eprint.insa-toulouse.fr/archive/00000315/.

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Dans le secteur biomédical et l’industrie agro-alimentaire, l’adhésion de microorganismes contaminants aux surfaces engendre de multiples impacts négatifs, à la fois en termes de santé publique, d’hygiène et de sécurité alimentaire. Dans ce contexte, l’objectif de l’étude est de mettre au point un traitement de surface de l’acier inoxydable 316L, afin de prévenir la colonisation microbienne. La modification des surfaces d’acier par traitement chimique ou physique n’a eu aucune incidence sur le détachement de Saccharomyces cerevisiae, évalué in vitro à l’aide d’une chambre à écoulement cisaillé. Les interactions entre la surface microbienne et les éléments métalliques du film passif semblent jouer un rôle prépondérant dans cette forte adhésion. Une stratégie originale, basée sur un procédé plasma couplant la polymérisation d’hexaméthyldisiloxane au bombardement d’une cible d’argent dans une décharge asymétrique radiofréquence, a ensuite été mise en œuvre et optimisée. Les surfaces d’acier ont ainsi été recouvertes de films minces (~ 175 nm) nanocomposites, constitués d’une matrice organosiliciée, présentant des propriétés anti-adhésives vis-à-vis de S. Cerevisiae, dans laquelle ont été incluses des nanoparticules d’argent, dotées d’une forte réactivité antimicrobienne. Le couplage de techniques d’analyse complémentaires, opérant à différentes échelles, a permis de corréler les caractéristiques des films nanocomposites à leur efficacité anti-adhésive et antifongique. Une inhibition totale de l’adhésion des levures a ainsi été obtenue, en augmentant le caractère polaire de la matrice, par ajout d’oxygène dans le plasma. En parallèle, un abattement de la viabilité de 1,9 log a été atteint sur les levures sessiles. La suite de l’étude a été dédiée à la compréhension des mécanismes d’action de l’argent, impliqués dans l’activité antifongique des films nanocomposites. Une inactivation de certaines protéines pariétales et intracellulaires, corrélée à des altérations de l’ultra-structure cellulaire, a ainsi été mise en évidence. La confirmation de l’activité biocide des films nanocomposites, sur deux modèles procaryotes (Staphylococcus aureus et Escherichia coli), a révélé par ailleurs la nécessité d’un contact étroit entre microorganismes et revêtement. Enfin, la stabilité des propriétés des films nanocomposites a été évaluée. Une utilisation répétée des dépôts a mis en évidence une réduction de l’activité antifongique, corrélée à une augmentation de l’efficacité anti-adhésive, liée au relargage d’argent lors de la première utilisation In the biomedical domain and the food industry, microbial adhesion to surfaces generates multiple negative consequences, in terms of human health, hygiene and safety of processed food. In this context, our approach is based on developing a 316L stainless steel surface treatment, to prevent microbial colonization. The surface modifications, mediated by chemical or physical treatment, did not promote Saccharomyces cerevisiae detachment, evaluated in vitro using a shear stress flow chamber. The interactions between the microbial surface and metallic elements of the passive film were hypothesized to play a predominant role in this strong adhesion. An original and dual strategy, based on a plasma process associating hexamethyldisiloxane polymerization and silver target bombardment in an asymmetrical radiofrequency discharge, was carried out and optimized. Stainless steel surfaces were thus coated with nanocomposite thin films (~ 175 nm), composed of an organosilicon matrix, exhibiting anti-adhesive properties towards S. Cerevisiae, in which were embedded silver nanoparticles, displaying a high antimicrobial reactivity. A large set of complementary analytical techniques, operating at different scales, was used to correlate nanocomposite film characteristics with their anti-adhesive and antimicrobial efficiency. A total inhibition of yeast cell adhesion was achieved, by increasing the matrix polar character, through oxygen addition during the plasma process. In parallel, a 1. 9 log reduction in viable counts was achieved for sessile yeast cells. Further experiments were dedicated to the thorough understanding of cellular changes induced by silver release. A deterioration of the secondary structure of proteins (cell wall, intracellular), combined with ultra-structure alterations, was observed. In addition, the biocide activity of the nanocomposite film was confirmed against two prokaryotic models (Staphylococcus aureus and Escherichia coli). The necessity of a direct contact between microorganisms and coating was demonstrated for a maximal antimicrobial efficiency. Lastly, the durability of the coating properties was assessed through a repeated use of the nanocomposite films. A decrease in the antifungal activity, coupled to an anti-adhesive property enhancement, was noticed and explained by the silver release during the first use

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Hart, Roger A. Bailey James E. Bailey James E. "Characterization of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli /." Diss., Pasadena, Calif. : California Institute of Technology, 1991. http://resolver.caltech.edu/CaltechETD:etd-06272007-152616.

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Olbrich, Richard. "The characterisation and recovery of protein inclusion bodies from recombinant Escherichia-coli." Thesis, University College London (University of London), 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.324583.

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Garcia, i. Fruitós Elena. "Regulation of recombinant proteína solubility and conformational quality in Escherichia coli." Doctoral thesis, Universitat Autònoma de Barcelona, 2008. http://hdl.handle.net/10803/3923.

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All the processes that take place in a cell require one or more proteins, meaning that they are essential components of life. Proteins are macromolecules consisting of amino acid units, all of them being constructed with combinations of only 20 amino acids. The primary structure of a protein molecule is determined by the sequence of amino acids connected by peptide bonds forming a polypeptide chain. Once the amino acid chain is synthesized, the protein folds by a physical process that might be eventually assisted by other proteins, reaching its characteristic three‐dimensional structure that is the final, functional conformation. However, although it is known that all the proteins must properly fold into their correct native conformation to be functional, their final conformation cannot be predicted from their primary amino acid sequence, being protein folding mechanisms one of the most challenging problems in biology today. Many proteins of relevant industrial or medical value are produced in low amounts in their natural sources. However, at the end of the seventies, the development of recombinant DNA technologies opened a new promising era for protein production in high amounts for both research and industrial applications. This had a tremendous impact, for example, in many areas of medicine as a tool to produce new drugs for the treatment of diseases and genetic disorders. Genetic engineering permits the introduction of the encoding genes of the protein of interest into recipient cells, where these genes are positioned downstream of regulable promoters in movable genetic elements, mainly plasmids. Under suitable conditions, these transgenic cells acting as protein production bio‐factories would be expected to act as unlimited and inexpensive source of rare, highly valuable proteins not only for proteomics and structural functional genomics1 but also for large‐scale preparative purposes. The quality as well as the quantity of the produced recombinant protein is greatly influenced by the chosen biological cell system. Bacteria have been the most commonly used organisms for protein production, specially the enterobacteria Escherichia coli, not only for the low cost of the used processes, but also for its fast growth. Generally, in Escherichia coli, the rather small host cell proteins can fold properly, adopting a native, biological active conformation. However, when producing heterologous proteins, specially those with eukaryotic or viral origin, important obstacles appear during the protein production process: a) in most cases, the protein is produced in a non functional conformation; b) sometimes the formed product is toxic for the cell; c) the protein often results proteolytically degraded2; d) the product is accumulated as an insoluble, non‐functional protein aggregates, known as inclusion bodies3. Therefore, even though the important advantages of the use of bacteria as a expression system, Escherichia coli also presents some drawbacks, such as its inability to carry most of the post‐transcriptional modifications, often required for eukaryotic protein function, the lack of a secretion mechanism to release the protein to the medium, and the inability to create an oxidative environment to facilitate disulfide bond formation required to achieve the final, functional structure of some proteins. Therefore, this leads to the production of proteins which are not always suitable for immediate use. This means that, to date, many proteins have been excluded from the biotechnological and pharmaceutical market because they cannot be produced in high yields as soluble and active products. To avoid protein folding problems encountered in bacteria under overexpression conditions, mainly secretion and post‐transcriptional modifications, alternative host cells, such as yeast, filamentous fungi, mammalian or insect cells, have been explored. Nevertheless, an enormous number of deficiencies in these systems such as difficulty of genetic manipulation, low productivity and high costs, shows that these organisms are not ideal for this aim and that, even when bacteria show some obstacles in the production process and often this system has to be optimized for specific products, it is, in most of the cases, the best choice.

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Mikkola, Isak. "Does SCP-2 promote the expression of foreign proteins in Escherichia coli?" Thesis, Linköpings universitet, Biologi, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-129802.

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Expression of foreign proteins in host organisms usually results in the development of insoluble, inactive proteins. Further, these proteins have a tendency to form aggregates termed inclusion bodies. However, the formation of inclusion bodies can be avoided by fusing the gene encoding the foreign protein to a highly soluble protein. In this report Sterol Carrier Protein-2 (SCP-2) is reviewed as a possible solubility tag. The experiment was carried out by fusing SCP-2 to one of two i nsoluble proteins, Green fluorescent protein (GFP) or a form of chloramphenicol acetyl transferase (CAT∆9). The protein fusion was then inserted into the vector pET-15b, transformed in Escherichia coli and the yield of actively expressed protein was measured. The results obtained from this study, as evaluated by PageBlue staining and Western blot, are indicating that SCP-2 does not improve the solubility of GFP or CAT∆9. Nonetheless, the solubility of GFP has earlier been increased by fusing it to the solubility tag maltose-binding protein (MBP). Producing more soluble forms of CAT∆9 have also been tested but without success. Therefore the conclusion drawn from this experiment is that SCP-2 does not work as a solubility tag, however more research must be performed to conclude this with certainty.

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Hedhammar, My. "Strategies for facilitated production of recombinant proteins in escherichia coli." Doctoral thesis, KTH, School of Biotechnology (BIO), 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-471.

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The successful genomic era has resulted in a great demand for efficient production and purification of proteins. The main objective of the work described in this thesis was to develop methods to facilitate recovery of target proteins after recombinant production in Escherichia coli.A positively charged purification tag, Zbasic, has previously been constructed by protein design of a compact three-helix bundle domain, Z. The charged domain was investigated for general use as a fusion partner. All target proteins investigated could be selectively captured by ion-exchange chromatography under conditions excluding adsorption of the majority of Escherichia coli host proteins. A single cation-exchange chromatography step at physiological pH was sufficient to provide Zbasic fusion proteins of high purity close to homogeneity. Moreover, efficient isolation directly from unclarified Escherichia coli homogenates could also be accomplished using an expanded bed mode. Since the intended use of a recombinant protein sometimes requires removal of the purification tag, a strategy for efficient release of the Zbasic moiety using an immobilised protease was developed. The protease columns were reusable without any measurable decrease in activity. Moreover, subsequent removal of the released tag, Zbasic, was effected by adsorption to a second cation-exchanger. Using a similar strategy, a purification tag with a negatively charged surface, denoted Zacid, was constructed and thoroughly characterised. Contrary to Zbasic, the negatively charged Zacid was highly unstructured in a low conductivity environment. Despite this, all Zacid fusion proteins investigated could be efficiently purified from whole cell lysates using anion-exchange chromatographySynthesis of polypeptides occurs readily in Escherichia coli providing large amounts of protein in cells of this type, albeit often one finds the recombinant proteins sequestered in inclusion bodies. Therefore, a high throughput method for screening of protein expression was developed. Levels of both soluble and precipitated protein could simultaneously be assessed in vivo by the use of a flow cytometer. The positively charged domain, Zbasic, was shown also to be selective under denaturing conditions, providing the possibility to purify proteins solubilised from inclusion bodies. Finally, a flexible process for solid-phase refolding was developed, using Zbasic as a reversible linker to the cation-exchanger resin.

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Libri sul tema "Escherichia coli Inclusions"

Henderson, Ian. Solving the inclusion body problem: A case study : high level expression of TEM-1 [beta]-lactamase in Escherichia coli. [s.l.]: typescript, 1993.

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Capitoli di libri sul tema "Escherichia coli Inclusions"

Garcìa-Fruitòs, Elena, Nuria Gonzàlez-Montalbàn, Mònica Martìnez-Alonso, Ursula Rinas, and Antonio Villaverde. "Systems-Level Analysis of Protein Quality in Inclusion Body-Forming Escherichia coli Cells." In Systems Biology and Biotechnology of Escherichia coli, 295–326. Dordrecht: Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-1-4020-9394-4_15.

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Williamson, Richard A. "Refolding of TIMP-2 from Escherichia coli Inclusion Bodies." In Methods in Molecular Biology, 111–21. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60327-299-5_7.

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Mouillac, Bernard, and Jean-Louis Banères. "Mammalian Membrane Receptors Expression as Inclusion Bodies in Escherichia coli." In Methods in Molecular Biology, 39–48. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-344-2_3.

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Panda, Amulya K. "Bioprocessing of Therapeutic Proteins from the Inclusion Bodies of Escherichia coli." In Biotechnology in India II, 43–93. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/3-540-36466-8_3.

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Lee, Wen-Chien, and Shao-Yen Hsu. "Over-Expression of Functionally Active Inclusion Bodies of Enzymes in Recombinant Escherichia coli." In Emerging Areas in Bioengineering, 21–33. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2018. http://dx.doi.org/10.1002/9783527803293.ch2.

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Burgess, Richard R. "[12] Purification of overproduced Escherichia coli RNA polymerase σ factors by solubilizing inclusion bodies and refolding from Sarkosyl." In Methods in Enzymology, 145–49. Elsevier, 1996. http://dx.doi.org/10.1016/s0076-6879(96)73014-8.

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