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

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Published: 2 June 2025

Last updated: 31 July 2025

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

DERRICK, JEREMY P., DALE B. WIGLEY, LU-YUN LIAN, et al. "Structure and mechanism of Streptococcal protein G." Biochemical Society Transactions 21, no. 4 (1993): 333S. http://dx.doi.org/10.1042/bst021333s.

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12

Gülich, Susanne, Martin Linhult, Stefan Ståhl, and Sophia Hober. "Engineering streptococcal protein G for increased alkaline stability." Protein Engineering, Design and Selection 15, no. 10 (2002): 835–42. http://dx.doi.org/10.1093/protein/15.10.835.

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13

ZHANG, HUCHENG, WEIFENG LIANG, HAITAO FAN, et al. "Immunological characterization and verification of recombinant streptococcal protein G." Molecular Medicine Reports 12, no. 4 (2015): 6311–15. http://dx.doi.org/10.3892/mmr.2015.4162.

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14

Derrick, Jeremy P., and Dale B. Wigley. "The Third IgG-Binding Domain from Streptococcal Protein G." Journal of Molecular Biology 243, no. 5 (1994): 906–18. http://dx.doi.org/10.1006/jmbi.1994.1691.

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15

Pelli, Afonso, Lucio R. Castellano, Marcos R. S. Cardoso, et al. "Differential reactivity of serum immunoglobulins from Brazilian wild mammals to staphylococcal A and streptococcal G proteins." Journal of Veterinary Diagnostic Investigation 24, no. 1 (2012): 148–52. http://dx.doi.org/10.1177/1040638711434322.

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Human pathogens have evolved to infect vertebrate hosts other than human beings without causing symptoms of the disease, thus permitting them to complete their life cycle and to develop into infectious forms. The identification and management of infected animals are alternatives to control dissemination of the disease and to prevent human illness. In the current study, the potential use of staphylococcal A or streptococcal G proteins was evaluated with enzyme-linked immunosorbent assays (ELISAs) for seroepidemiological studies. Sera were collected from animals that were representative of 23 di

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16

Goward, C. R., J. P. Murphy, T. Atkinson, and D. A. Barstow. "Expression and purification of a truncated recombinant streptococcal protein G." Biochemical Journal 267, no. 1 (1990): 171–77. http://dx.doi.org/10.1042/bj2670171.

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The gene for Protein G from Streptococcus strain G148 was cloned and expressed in Escherichia coli. The regions on the gene corresponding to the albumin-binding domains and the Fab-binding region were then deleted by site-directed mutagenesis. The translation of regions corresponding to the cell-wall- and membrane-binding domains was prevented by introduction of stop codons upstream of these domains. This recombinant DNA sequence codes for a protein (G′) that contains repetitive regions and that binds only the Fc portion of IgG, analogously to Protein A. Translation of the sequence produces a

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17

Stephens, Michael E., Terri N. Ellis, Jay S. Huebner, Erica M. Kelly, and Doria F. Bowers. "Streptococcal Protein G Enhances Antibody Binding to Platinum Sensor Surfaces." Journal of Sensor Technology 05, no. 01 (2015): 1–6. http://dx.doi.org/10.4236/jst.2015.51001.

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18

Gronenborn, Angela M., and G. Marius Clore. "Structural Studies of Immunoglobulin-Binding Domains of Streptococcal Protein G." ImmunoMethods 2, no. 1 (1993): 3–8. http://dx.doi.org/10.1006/immu.1993.1002.

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19

Guss, B., M. Eliasson, A. Olsson, et al. "Structure of the IgG-binding regions of streptococcal protein G." EMBO Journal 5, no. 7 (1986): 1567–75. http://dx.doi.org/10.1002/j.1460-2075.1986.tb04398.x.

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20

Tian, Xiaojie, Min Wang, Kaiyuan Zhang, and Xinqing Zhang. "Novel SPG 11 Mutations in Hereditary Spastic Paraplegia With Thin Corpus Callosum in a Chinese Family." Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 43, no. 6 (2016): 833–40. http://dx.doi.org/10.1017/cjn.2016.17.

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AbstractBackground: Hereditary spastic paraplegia (HSP) is a neurodegenerative disease that is characterized by progressive weakness and spasticity of the lower extremities; HSP can present as complicated forms with additional neurological signs. More than 70 disease loci have been described with different modes of inheritance. Methods: In this study, nine subjects from a Chinese family that included two individuals affected by HSP were examined through detailed clinical evaluations, physical examinations, and genetic tests. Targeted exome capture technology was used to identify gene mutations

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21

Eliasson, M., A. Olsson, E. Palmcrantz, et al. "Chimeric IgG-binding receptors engineered from staphylococcal protein A and streptococcal protein G." Journal of Biological Chemistry 263, no. 9 (1988): 4323–27. http://dx.doi.org/10.1016/s0021-9258(18)68928-8.

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22

Jain, Nemi C., J. L. Vegad, and C. S. Kono. "Methods for detection of immune-mediated neutropenia in horses, using antineutrophil serum of rabbit origin." American Journal of Veterinary Research 51, no. 7 (1990): 1026–31. http://dx.doi.org/10.2460/ajvr.1990.51.07.1026.

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SUMMARY Equine neutrophil antibody was raised in rabbits inoculated with equine neutrophils isolated to purity > 99.0%, using Percoll density-gradient sedimentation. Neutrophil antibody was detected by use of agar gel diffusion, leukoagglutination, indirect immunofluorescence, staphylococcal protein A and streptococcal protein G binding, and phagocytic inhibition techniques. Precipitin lines and leukoagglutination were seen in antiserum dilutions of 1:4 and 1:64, respectively. The specific nature of leukoagglutination was characterized by the formation of rosette-like clumps of neutrophils.

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23

Hatan, Meital, Vera Shinder, David Israeli, Frank Schnorrer, and Talila Volk. "The Drosophila blood brain barrier is maintained by GPCR-dependent dynamic actin structures." Journal of Cell Biology 192, no. 2 (2011): 307–19. http://dx.doi.org/10.1083/jcb.201007095.

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The blood brain barrier (BBB) is essential for insulation of the nervous system from the surrounding environment. In Drosophila melanogaster, the BBB is maintained by septate junctions formed between subperineurial glia (SPG) and requires the Moody/G protein–coupled receptor (GPCR) signaling pathway. In this study, we describe novel specialized actin-rich structures (ARSs) that dynamically form along the lateral borders of the SPG cells. ARS formation and association with nonmuscle myosin is regulated by Moody/GPCR signaling and requires myosin activation. Consistently, an overlap between ARS

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24

Zhao, Wei, Dong Yu, Jian-guo Cheng, et al. "Affinity of Streptococcal G Protein to Forest Musk Deer (Moschus berezovskii) Serum Immunoglobulin G." Journal of Wildlife Diseases 56, no. 3 (2020): 684. http://dx.doi.org/10.7589/2019-09-223.

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25

Sjöbring, U., C. Falkenberg, E. Nielsen, B. Akerström, and L. Björck. "Isolation and characterization of a 14-kDa albumin-binding fragment of streptococcal protein G." Journal of Immunology 140, no. 5 (1988): 1595–99. http://dx.doi.org/10.4049/jimmunol.140.5.1595.

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Abstract Protein G, a streptococcal cell wall protein, has separate binding sites for human albumin and IgG. Streptococci expressing protein G were treated with the bacteriolytic agent mutanolysin. Several IgG- and human serum albumin (HSA)-binding peptides were identified in the material thus solubilized and one of these, a 14-kDa peptide, was found to bind HSA but not IgG in Western blot experiments. This molecule was purified by affinity chromatography on Sepharose coupled with HSA followed by gel filtration on Sepharose 6B and a final affinity chromatography on IgG-Sepharose, by which low

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26

OLSSON, Anders, Margareta ELIASSON, Bengt GUSS, et al. "Structure and evolution of the repetitive gene encoding streptococcal protein G." European Journal of Biochemistry 168, no. 2 (1987): 319–24. http://dx.doi.org/10.1111/j.1432-1033.1987.tb13423.x.

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27

Akerström, B., E. Nielsen, and L. Björck. "Definition of IgG- and albumin-binding regions of streptococcal protein G." Journal of Biological Chemistry 262, no. 28 (1987): 13388–91. http://dx.doi.org/10.1016/s0021-9258(19)76438-2.

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28

PALMER, B., K. ANGUS, L. TAYLOR, J. WARWICKER, and J. DERRICK. "Design of stability at extreme alkaline pH in streptococcal protein G." Journal of Biotechnology 134, no. 3-4 (2008): 222–30. http://dx.doi.org/10.1016/j.jbiotec.2007.12.009.

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29

Li, Qi, Hai-Ning Du, and Hong-Yu Hu. "Study of protein-protein interactions by fluorescence of tryptophan analogs: Application to immunoglobulin G binding domain of streptococcal protein G." Biopolymers 72, no. 2 (2003): 116–22. http://dx.doi.org/10.1002/bip.10300.

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30

Miller, Craig W., John F. Prescott, Karol A. Mathews, et al. "Streptococcal toxic shock syndrome in dogs." Journal of the American Veterinary Medical Association 209, no. 8 (1996): 1421–26. http://dx.doi.org/10.2460/javma.1996.209.08.1421.

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Objective To determine the clinical, pathologic, and bacteriologic findings in dogs that developed severe invasive infections with group G streptococci (GGS) over a 6-month period in southern Ontario. Design Prospective case series. Animals 7 dogs in southern Ontario with severe streptococcal infection during a 6-month period. Procedure Using pulsed-field gel electrophoresis, molecular typing of streptococcal isolates was performed. Isolates were examined for the M protein gene emm1.0, pyrogenic exotoxin genes speA, speB, speF, hyaluronic acid synthase genes hasA, hasB, and for C5a peptidase g

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31

Lee, Hae Gon, Shinill Kang, and Joon Sang Lee. "Binding characteristics of staphylococcal protein A and streptococcal protein G for fragment crystallizable portion of human immunoglobulin G." Computational and Structural Biotechnology Journal 19 (2021): 3372–83. http://dx.doi.org/10.1016/j.csbj.2021.05.048.

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32

Nilson, Bo, Lars Björck, and Bo Åkerström. "Enzyme Linked Immunosorbent Assay Using Alkaline Phosphatase Conjugated with Streptococcal Protein G." Journal of Immunoassay 9, no. 2 (1988): 207–25. http://dx.doi.org/10.1080/15321818808057041.

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33

NYGREN, Per-Ake, Charlotta LJUNGQUIST, Hanne TROMBORG, Kjell NUSTAD, and Mathias UHLEN. "Species-dependent binding of serum albumins to the streptococcal receptor protein G." European Journal of Biochemistry 193, no. 1 (1990): 143–48. http://dx.doi.org/10.1111/j.1432-1033.1990.tb19315.x.

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34

Murphy, Duane A., William Van Alstine, Terry Bowersock, and Cesar Burgos. "Binding of a Recombinant form of Streptococcal Protein G to Porcine IgG." Journal of Veterinary Diagnostic Investigation 4, no. 4 (1992): 469–70. http://dx.doi.org/10.1177/104063879200400422.

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35

Kitsiouli, Eirini, Marilena E. Lekka, George Nakos, Claude Cassagne, and Lilly Maneta-Peyret. "Lipids are co-eluted with immunoglobulins G during purification by recombinant streptococcal protein G affinity chromatography." Journal of Immunological Methods 271, no. 1-2 (2002): 107–11. http://dx.doi.org/10.1016/s0022-1759(02)00345-9.

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36

Goodfellow, Alison M., Megan Hibble, Susanne R. Talay, et al. "Distribution and Antigenicity of Fibronectin Binding Proteins (SfbI and SfbII) of Streptococcus pyogenes Clinical Isolates from the Northern Territory, Australia." Journal of Clinical Microbiology 38, no. 1 (2000): 389–92. http://dx.doi.org/10.1128/jcm.38.1.389-392.2000.

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ABSTRACT Fibronectin binding proteins play an important role in the adherence and invasion of group A streptococci (GAS). Genotypically distinct GAS isolates were screened for the presence and expression of two streptococcal fibronectin binding protein genes, sfbI and sfbII . Of the tested strains, 64 and 36% were shown to harbor and express the sfbI and sfbII genes, respectively. All sfbII -positive strains tested were also positive for sfbI , but only 28% of the sfbII -negative strains were positive for sfbI . High levels of immunoglobulin G antibodies to both SfbI and SfbII were found in se

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37

Goward, C. R., L. I. Irons, J. P. Murphy, and T. Atkinson. "The secondary structure of protein G′, a robust molecule." Biochemical Journal 274, no. 2 (1991): 503–7. http://dx.doi.org/10.1042/bj2740503.

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The secondary structure of recombinant streptococcal Protein G' was predicted and compared with spectropolarimetric data. The predicted secondary structure consisted of 37 +/- 4% alpha-helix and 30 +/- 5% beta-sheet, whereas the values obtained from c.d. data were 29 +/- 2% alpha-helix and 41 +/- 3% beta-sheet. An alpha-helix-beta-sheet/turn-alpha-helix motif is conjectured to comprise the Fc-binding unit. The c.d. spectra in the near u.v. and far u.v. show that the Protein G' molecule is stable to heating at 100 degrees C and to extremes of pH (pH 1.5 to 11.0). The protein retained biological

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38

Derrick, Jeremy P., and Dale B. Wigley. "Crystal structure of a streptococcal protein G domain bound to an Fab fragment." Nature 359, no. 6397 (1992): 752–54. http://dx.doi.org/10.1038/359752a0.

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39

Nygren, Per-Åke, Margareta Eliasson, Lars Abrahmsén, Mathias Uhlén, and Elisabeth Palmcrantz. "Analysis and use of the serum albumin binding domains of streptococcal protein G." Journal of Molecular Recognition 1, no. 2 (1988): 69–74. http://dx.doi.org/10.1002/jmr.300010204.

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40

Sjöbring, U., J. Trojnar, A. Grubb, B. Akerström, and L. Björck. "Ig-binding bacterial proteins also bind proteinase inhibitors." Journal of Immunology 143, no. 9 (1989): 2948–54. http://dx.doi.org/10.4049/jimmunol.143.9.2948.

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Abstract Protein G is a streptococcal cell wall protein with separate binding sites for IgG and human serum albumin (HSA). In the present work it was demonstrated that alpha 2-macroglobulin (alpha 2M) and kininogen, two proteinase inhibitors of human plasma, bound to protein G, whereas 23 other human proteins showed no affinity. alpha 2M was found to interact with the IgG-binding domains of protein G, and in excess alpha 2M inhibited IgG binding and vice versa. A synthetic peptide, corresponding to one of the homologous IgG-binding domains of protein G, blocked binding of protein G to alpha 2M

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41

Nitsche-Schmitz, D. Patric, Helena M. Johansson, Inka Sastalla, Silvana Reissmann, Inga-Maria Frick, and Gursharan S. Chhatwal. "Group G Streptococcal IgG Binding Molecules FOG and Protein G Have Different Impacts on Opsonization by C1q." Journal of Biological Chemistry 282, no. 24 (2007): 17530–36. http://dx.doi.org/10.1074/jbc.m702612200.

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42

Lindhqvist, Violetta, Ulf Niss, and Rune Nilsson. "Comparison of the Mitogenic Activities of Streptococcal Protein-G and Staphylococcal Protein-A on Human Mononuclear Cells." Immunological Investigations 18, no. 7 (1989): 919–30. http://dx.doi.org/10.3109/08820138909050770.

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43

Gronenborn, A., D. Filpula, N. Essig, et al. "A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G." Science 253, no. 5020 (1991): 657–61. http://dx.doi.org/10.1126/science.1871600.

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44

Proudfoot, Karen A., Christopher Torrance, Alastair D. G. Lawson, and David J. King. "Purification of recombinant chimeric B72.3 Fab′ and F(ab′)2 using streptococcal protein G." Protein Expression and Purification 3, no. 5 (1992): 368–73. http://dx.doi.org/10.1016/s1046-5928(05)80037-3.

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45

Erntell, Mats, Erling B. Myhre, Ulf Sjöbring, and Lars Björck. "Streptococcal protein G has affinity for both Fab- and Fc-fragments of human IgG." Molecular Immunology 25, no. 2 (1988): 121–26. http://dx.doi.org/10.1016/0161-5890(88)90059-4.

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46

Kuszewski, John, G. Marius Clore, and Angela M. Gronenborn. "Fast folding of a prototypic polypeptide: The immunoglobulin binding domain of streptococcal protein G." Protein Science 3, no. 11 (1994): 1945–52. http://dx.doi.org/10.1002/pro.5560031106.

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47

Horii, Toshinobu, Sayuri Izumida, Kiyotake Takeuchi, Toyohiro Tada, Jinko Ishikawa та Koji Tsuboi. "Acute peritonitis and salpingitis associated with streptococcal toxic shock syndrome caused by Lancefield group G α-haemolytic Streptococcus dysgalactiae subsp. equisimilis". Journal of Medical Microbiology 55, № 7 (2006): 953–56. http://dx.doi.org/10.1099/jmm.0.46507-0.

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The authors treated a patient for what appears to be the first reported occurrence of acute peritonitis and salpingitis associated with streptococcal toxic shock syndrome (STSS). This was caused by Lancefield group G α-haemolytic Streptococcus dysgalactiae subsp. equisimilis TKCH2004-001. The isolate showed M protein type stc36 and carried the spegg gene. To the best of the authors' knowledge, the present report represents the first case of STSS complicating acute peritonitis and salpingitis caused by Lancefield group G α-haemolytic S. dysgalactiae subsp. equisimilis.

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48

Du, Hai-Ning, Tie-Ying Zhang, Yong-Gang Chang, Dong-Hai Lin, and Hong-Yu Hu. "Effects of segment substitution on the structure and stability of immunoglobulin G binding domain of streptococcal protein G." Biopolymers 79, no. 1 (2005): 9–17. http://dx.doi.org/10.1002/bip.20283.

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49

Gomi, H., T. Hozumi, S. Hattori, C. Tagawa, F. Kishimoto, and L. Björck. "The gene sequence and some properties of protein H. A novel IgG-binding protein." Journal of Immunology 144, no. 10 (1990): 4046–52. http://dx.doi.org/10.4049/jimmunol.144.10.4046.

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Abstract The gene for protein H, a novel bacterial cell wall protein with specific affinity for human IgG Fc, was cloned from a group A Streptococcus and expressed in Escherichia coli. Recombinant E. coli cells produced two forms of a human IgG Fc-binding protein, one with an apparent Mr of 42 kDa in a periplasmic fraction and the other with an apparent Mr of 45 kDa in a mixed fraction of cytoplasms and membranes. Both 42-kDa and 45-kDa protein preparations similarly bound to human IgG1 to IgG4, human IgG Fc, and rabbit IgG, but not to IgG of mouse, rat, bovine, sheep, goat, and human IgA, IgD

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50

Stenberg, L., P. W. O'Toole, J. Mestecky, and G. Lindahl. "Molecular characterization of protein Sir, a streptococcal cell surface protein that binds both immunoglobulin A and immunoglobulin G." Journal of Biological Chemistry 269, no. 18 (1994): 13458–64. http://dx.doi.org/10.1016/s0021-9258(17)36854-0.

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