S. aureus IgG-binding proteins SpA and Sbi: Host specificity and mechanisms of immune complex formation

Atkins, Karen; Burman, Julia D.; Chamberlain, Emily S.; Cooper, Jessica E.; Poutrel, B.; Bagby, Stefan; Jenkins, A. Toby A.; Feil, Edward J.; Elsen, Jean M. H. van den

doi:10.1016/j.molimm.2007.10.021

Cited by 127 publications

(106 citation statements)

References 29 publications

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“…Nevertheless, Burman and colleagues showed that Sbi is extracellular, and they suggested that cell surface-bound Sbi might be disadvantageous for the bacterium due to its role in modulating the complement system (8). On the other hand, cell surface localization of Sbi would be appropriate for interference with the adaptive immune system through IgG binding (3). Irrespective of these previously reported findings, our Western blotting analyses show that Sbi is noncovalently bound to the cell wall, not only in S. aureus SH1000 and S. aureus RN4220 but also in S. aureus Newman.…”

Section: Discussioncontrasting

confidence: 40%

Synthetic Effects ofsecGandsecY2Mutations on Exoproteome Biogenesis inStaphylococcus aureus

et al. 2010

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The Gram-positive pathogen Staphylococcus aureus secretes various proteins into its extracellular milieu. Bioinformatics analyses have indicated that most of these proteins are directed to the canonical Sec pathway, which consists of the translocation motor SecA and a membrane-embedded channel composed of the SecY, SecE, and SecG proteins. In addition, S. aureus contains an accessory Sec2 pathway involving the SecA2 and SecY2 proteins. Here, we have addressed the roles of the nonessential channel components SecG and SecY2 in the biogenesis of the extracellular proteome of S. aureus. The results show that SecG is of major importance for protein secretion by S. aureus. Specifically, the extracellular accumulation of nine abundant exoproteins and seven cell wall-bound proteins was significantly affected in an secG mutant. No secretion defects were detected for strains with a secY2 single mutation. However, deletion of secY2 exacerbated the secretion defects of secG mutants, affecting the extracellular accumulation of one additional exoprotein and one cell wall protein. Furthermore, an secG secY2 double mutant displayed a synthetic growth defect. This might relate to a slightly elevated expression of sraP, encoding the only known substrate for the Sec2 pathway, in cells lacking SecG. Additionally, the results suggest that SecY2 can interact with the Sec1 channel, which would be consistent with the presence of a single set of secE and secG genes in S. aureus.

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Section: Discussioncontrasting

confidence: 40%

Synthetic Effects ofsecGandsecY2Mutations on Exoproteome Biogenesis inStaphylococcus aureus

et al. 2010

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“…Most bacterial immunoglobulin-binding proteins exhibit little or no sequence homology and are generally considered to have converged during evolution to bind overlapping sites in the interdomain region, with the observed diversity in immunoglobulin-binding profiles with respect to isotype, subclass and species being accounted for by the different binding interactions (Frick et al, 1992;Goward et al, 1993;Pleass et al, 2001). The best studied IgG-binding proteins are protein A and protein G. Protein G and protein G-like proteins are responsible for much of the IgG binding by group C and group G streptococci (Björck et al, 1987;Navarre & Schneewind, 1999), whereas IgG binding by Staphylococcus aureus is mediated by protein A and/or Sbi, a protein A-like protein (Atkins et al, 2008;Moks et al, 1986;Uhlén et al, 1984). In S. pyogenes, immunoglobulin binding is mediated by three groups of M proteins encoded by the emm, mrp and enn genes.…”

Section: Introductionmentioning

confidence: 99%

Localization of the equine IgG-binding domain in the fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi

et al. 2009

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Fibrinogen-binding protein (FgBP, also termed SeM) is a cell-wall-associated anti-phagocytic M-like protein of the equine pathogen Streptococcus equi subsp. equi, and binds fibrinogen (Fg) and IgG. FgBP binds Fg avidly through residues located at the extreme N terminus of the molecule, whereas the IgG-binding site is more centrally located between the A and B repeats. FgBP binds equine IgG4 and IgG7 subclasses through interaction with the CH2–CH3 interdomain region of IgG-Fc, and possesses overlapping Fc-binding sites with protein A and protein G. In this study, FgBP truncates containing defined internal deletions were used to identify a stretch of 14 aa (residues 335–348) critical for IgG binding. Protein chimeras consisting of the non-IgG-binding α-helical coiled-coil M5 protein fused to FgBP sequences were used to identify a minimal equine IgG-binding domain consisting of residues 329–360. Competition ELISA tests suggested that IgG does not compromise Fg binding and vice versa.

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“…The cell wall-anchored protein A and secreted protein Sbi share many of the same characteristics, targeting IgG from a number of different species and subclass types predominantly at the Fc domain (45,46). SSL10 appears to favor the upper Cg2 domain, whereas the CH2/CH3 interface serves as the primary target for a number of unrelated Ig binding proteins across many different bacterial species (19,22,39,43,47).…”

Section: Discussionmentioning

confidence: 99%

Specificity of Staphylococcal Superantigen-Like Protein 10 toward the Human IgG1 Fc Domain

Patel

Wines

Langley

et al. 2010

The Journal of Immunology

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S. aureus IgG-binding proteins SpA and Sbi: Host specificity and mechanisms of immune complex formation

Cited by 127 publications

References 29 publications

Synthetic Effects ofsecGandsecY2Mutations on Exoproteome Biogenesis inStaphylococcus aureus

Synthetic Effects ofsecGandsecY2Mutations on Exoproteome Biogenesis inStaphylococcus aureus

Localization of the equine IgG-binding domain in the fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi

Specificity of Staphylococcal Superantigen-Like Protein 10 toward the Human IgG1 Fc Domain

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