Relevant bibliographies by topics / Streptococcal protein G (SpG)

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Streptococcal protein G (SpG)'

Author: Grafiati
Published: 2 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "Streptococcal protein G (SpG)"

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Eliasson, M., R. Andersson, A. Olsson, H. Wigzell, and M. Uhlén. "Differential IgG-binding characteristics of staphylococcal protein A, streptococcal protein G, and a chimeric protein AG." Journal of Immunology 142, no. 2 (1989): 575–81. http://dx.doi.org/10.4049/jimmunol.142.2.575.

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Abstract Various Gram-positive bacteria express different types of IgG-binding receptors, each of which displaying certain unique binding properties. To evaluate specificity and avidity aspects of the differential binding pattern, a set of competitive binding assays was employed, by using staphylococcal protein A (SPA), streptococcal protein G (SPG), and a chimeric protein AG. These receptors were analyzed, in a reciprocal fashion, for binding and inhibition of binding to a selected panel of polyclonal and monoclonal Ig. Results of the study reveal that a majority of the determinants on human
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Ling, Wei-Li, Joshua Yi Yeo, Yuen-Ling Ng, Anil Wipat, and Samuel Ken-En Gan. "More Than Meets the Kappa for Antibody Superantigen Protein L (PpL)." Antibodies 11, no. 1 (2022): 14. http://dx.doi.org/10.3390/antib11010014.

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Immunoglobulin superantigens play an important role in affinity purification of antibodies and the microbiota-immune axis at mucosal areas. Based on current understanding, Staphylococcal Protein A (SpA), Streptococcal Protein G (SpG) and Finegoldia Protein L (PpL) are thought to only bind specific regions of human antibodies, allowing for selective purification of antibody isotypes and chains. Clinically, these superantigens are often classified as toxins and increase the virulence of the producing pathogen through unspecific interactions with immune proteins. To perform an in-depth interactio
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Munson, Sibyl H., Mary T. Tremaine, Marsha J. Betley, and Rodney A. Welch. "Identification and Characterization of Staphylococcal Enterotoxin Types G and I fromStaphylococcus aureus." Infection and Immunity 66, no. 7 (1998): 3337–48. http://dx.doi.org/10.1128/iai.66.7.3337-3348.1998.

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ABSTRACT Staphylococcal enterotoxins are exotoxins produced byStaphylococcus aureus that possess emetic and superantigenic properties. Prior to this research there were six characterized enterotoxins, staphylococcal enterotoxin types A to E and H (referred to as SEA to SEE and SEH). Two new staphylococcal enterotoxin genes have been identified and designated segand sei (staphylococcal enterotoxin types G and I, respectively). seg and sei consist of 777 and 729 nucleotides, respectively, encoding precursor proteins of 258 (SEG) and 242 (SEI) deduced amino acids. SEG and SEI have typical bacteri
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Proft, Thomas, S. Louise Moffatt, Celia J. Berkahn, and John D. Fraser. "Identification and Characterization of Novel Superantigens from Streptococcus pyogenes." Journal of Experimental Medicine 189, no. 1 (1999): 89–102. http://dx.doi.org/10.1084/jem.189.1.89.

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Three novel streptococcal superantigen genes (spe-g, spe-h, and spe-j) were identified from the Streptococcus pyogenes M1 genomic database at the University of Oklahoma. A fourth novel gene (smez-2) was isolated from the S. pyogenes strain 2035, based on sequence homology to the streptococcal mitogenic exotoxin z (smez) gene. SMEZ-2, SPE-G, and SPE-J are most closely related to SMEZ and streptococcal pyrogenic exotoxin (SPE)-C, whereas SPE-H is most similar to the staphylococcal toxins than to any other streptococcal toxin. Recombinant (r)SMEZ, rSMEZ-2, rSPE-G, and rSPE-H were mitogenic for hu
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Baev, Didi, Reg England, and Howard K. Kuramitsu. "Stress-Induced Membrane Association of the Streptococcus mutans GTP-Binding Protein, an Essential G Protein, and Investigation of Its Physiological Role by Utilizing an Antisense RNA Strategy." Infection and Immunity 67, no. 9 (1999): 4510–16. http://dx.doi.org/10.1128/iai.67.9.4510-4516.1999.

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ABSTRACT SGP (for Streptococcus GTP-binding protein) is aStreptococcus mutans essential GTPase which has significant sequence identity to the previously identified Escherichia coli Era protein and to numerous other prokaryotic GTPase proteins of unknown function. Recent studies in our laboratory have addressed the possible role of SGP in the stress response of the oral pathogen S. mutans. Here we report that during growth in the early stationary phase, and in response to elevated temperatures or acidic pH, the distribution of SGP between the cytoplasm and the membranes of S. mutans cells varie
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Burova, L. A., A. N. Suvorov, and A. A. Totolian. "Streptococcus pyogenes: phenomenon of nonimmune binding of human immunoglobulins and its role in pathology." Medical Immunology (Russia) 24, no. 2 (2022): 217–34. http://dx.doi.org/10.15789/1563-0625-spp-2450.

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M and M-like proteins represent the main pathogenicity factors of Streptococcus pyogenes, a widely spread and potentially lethal bacterial pathogen. These proteins provide resistance of the microbe to innate and adaptive immune response, due to attraction of specific human proteins to the streptococcal surface. Nonimmune binding of immunoglobulins G (IgG) and A (IgA) via their Fc domains to M and M-like proteins was described over 40 years ago, but its role for the pathogenicity of Streptococcus pyogenes is far from definite resolution. The discovery of this phenomenon should be considered amo
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Burova, L. A., A. N. Suvorov, and A. A. Totolian. "Streptococcus pyogenes: phenomenon of nonimmune binding of human immunoglobulins and its role in pathology." Medical Immunology (Russia) 24, no. 2 (2022): 217–34. http://dx.doi.org/10.15789/1563-0625-spp-2450.

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M and M-like proteins represent the main pathogenicity factors of Streptococcus pyogenes, a widely spread and potentially lethal bacterial pathogen. These proteins provide resistance of the microbe to innate and adaptive immune response, due to attraction of specific human proteins to the streptococcal surface. Nonimmune binding of immunoglobulins G (IgG) and A (IgA) via their Fc domains to M and M-like proteins was described over 40 years ago, but its role for the pathogenicity of Streptococcus pyogenes is far from definite resolution. The discovery of this phenomenon should be considered amo
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Fahnestock, Stephen R. "Cloned streptococcal protein G genes." Trends in Biotechnology 5, no. 3 (1987): 79–83. http://dx.doi.org/10.1016/s0167-7799(87)80016-1.

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Wu, J., M. I. Cho, and H. K. Kuramitsu. "Expression, purification, and characterization of a novel G protein, SGP, from Streptococcus mutans." Infection and immunity 63, no. 7 (1995): 2516–21. http://dx.doi.org/10.1128/iai.63.7.2516-2521.1995.

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Sjöbring, U., L. Björck, and W. Kastern. "Streptococcal protein G. Gene structure and protein binding properties." Journal of Biological Chemistry 266, no. 1 (1991): 399–405. http://dx.doi.org/10.1016/s0021-9258(18)52448-0.

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Dissertations / Theses on the topic "Streptococcal protein G (SpG)"

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Dwivedi, Gaurav Dutta. "Cloning and Expression of Streptococcal Recombinant Protein G." Thesis, Umeå universitet, Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet), 2015. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-106723.

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Recombinant Protein G (rPG), an engineered form of streptococcal protein G with a theoretical molecular weight of 22.26 kDa was successfully cloned and expressed in E.coli BL 21(DE3) cells. The albumin binding domain was removed during the gene synthesis to avoid unspecific binding. This recombinant form of protein G contains only the IgG binding domains along with the 6X histidine tag at the N terminal. The removal of non-specific domains maximizes the specificity of IgG binding through the Fc region. The recombinant protein G was purified through heat treatment and using immobilized metal af
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McCabe, Christie Renee. "A novel antibody based capture matrix utilizing human serum albumin and streptococcal Protein G to increase capture efficiency of bacteria." [Tampa, Fla] : University of South Florida, 2009. http://purl.fcla.edu/usf/dc/et/SFE0002811.

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Gülich, Susanne. "Engineering Proteinaceous Ligands for Improved Performance in Affinity Chromatography Applications." Doctoral thesis, KTH, Biotechnology, 2002. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-3327.

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Cnudde, Sara Elizabeth. "The x-ray crystallographic structures of the angiogenesis inhibitor angiostatin bound to a peptide from the group A streptococcal surface protein PAM and the metal-bound conantokins con-G and con-T[K7gamma]." Diss., Connect to online resource - MSU authorized users, 2007.

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Book chapters on the topic "Streptococcal protein G (SpG)"

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Björck, Lars, and Bo Åkerström. "Streptococcal protein G." In Bacterial Immunoglobulin-binding Proteins. Elsevier, 1990. http://dx.doi.org/10.1016/b978-0-12-123011-1.50013-7.

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Fahnestock, Stephen R., and Patrick Alexander. "The cloning of streptococcal protein G genes." In Bacterial Immunoglobulin-Binding Proteins. Elsevier, 1990. http://dx.doi.org/10.1016/b978-0-12-123012-8.50028-4.

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Fahnestock, Stephen R., Patrick Alexander, David Filpula, and James Nagle. "Structure and evolution of the streptococcal genes encoding protein G." In Bacterial Immunoglobulin-binding Proteins. Elsevier, 1990. http://dx.doi.org/10.1016/b978-0-12-123011-1.50015-0.

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Zhang, Hucheng, Weifeng Liang, Haitao Fan, et al. "Determination of Immunological Characterization and Verification of Recombinant Streptococcal Protein G." In New Visions in Biological Science Vol. 10. Book Publisher International (a part of SCIENCEDOMAIN International), 2022. http://dx.doi.org/10.9734/bpi/nvbs/v10/3515e.

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VK, Anand, and Shanthi G. "Production and Characterization of Valuable Protein Hydrolysates from De-Oiled Residual Biomass-Spirulina Platensis." In Emerging Food and Bioscience Research on Human Health: Safety, Security and Sustainable Aspects. Skyfox Publishing Group, 2023. http://dx.doi.org/10.22573/spg.023.978-93-90357-85-7/4.

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There is growing curiosity in the exploration of novel renewable resources as alternatives for the production of protein hydrolysates (PH). Thus, the undiscovered potential of utilizing residual biomass from Spirulina, particularly after lipid extraction, for food production presents an encouraging avenue for further research. The aim of this study is to examine the technological and antioxidant properties of protein hydrolysates (PH) obtained from the leftover biomass of Spirulina. Around 70% of biomass was obtained as residue after lipid extraction. The yield and protein content of the PH fr
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Journal articles
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