2.50
Hdl Handle:
http://hdl.handle.net/10033/621217
Title:
SCM, the M Protein of Streptococcus canis Binds Immunoglobulin G.
Authors:
Bergmann, Simone; Eichhorn, Inga; Kohler, Thomas P; Hammerschmidt, Sven; Goldmann, Oliver; Rohde, Manfred ( 0000-0003-0522-3580 ) ; Fulde, Marcus
Abstract:
The M protein of Streptococcus canis (SCM) is a virulence factor and serves as a surface-associated receptor with a particular affinity for mini-plasminogen, a cleavage product of the broad-spectrum serine protease plasmin. Here, we report that SCM has an additional high-affinity immunoglobulin G (IgG) binding activity. The ability of a particular S. canis isolate to bind to IgG significantly correlates with a scm-positive phenotype, suggesting a dominant role of SCM as an IgG receptor. Subsequent heterologous expression of SCM in non-IgG binding S. gordonii and Western Blot analysis with purified recombinant SCM proteins confirmed its IgG receptor function. As expected for a zoonotic agent, the SCM-IgG interaction is species-unspecific, with a particular affinity of SCM for IgGs derived from human, cats, dogs, horses, mice, and rabbits, but not from cows and goats. Similar to other streptococcal IgG-binding proteins, the interaction between SCM and IgG occurs via the conserved Fc domain and is, therefore, non-opsonic. Interestingly, the interaction between SCM and IgG-Fc on the bacterial surface specifically prevents opsonization by C1q, which might constitute another anti-phagocytic mechanism of SCM. Extensive binding analyses with a variety of different truncated SCM fragments defined a region of 52 amino acids located in the central part of the mature SCM protein which is important for IgG binding. This binding region is highly conserved among SCM proteins derived from different S. canis isolates but differs significantly from IgG-Fc receptors of S. pyogenes and S. dysgalactiae sub. equisimilis, respectively. In summary, we present an additional role of SCM in the pathogen-host interaction of S. canis. The detailed analysis of the SCM-IgG interaction should contribute to a better understanding of the complex roles of M proteins in streptococcal pathogenesis.
Affiliation:
Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr.7, 38124 Braunschweig, Germany.
Citation:
SCM, the M Protein of Streptococcus canis Binds Immunoglobulin G. 2017, 7:80 Front Cell Infect Microbiol
Journal:
Frontiers in cellular and infection microbiology
Issue Date:
2017
URI:
http://hdl.handle.net/10033/621217
DOI:
10.3389/fcimb.2017.00080
PubMed ID:
28401063
Type:
Article
Language:
en
ISSN:
2235-2988
Appears in Collections:
publications of the research group immunology of infection (INI); publications of the central unit for microscopy (ZEIM)

Full metadata record

DC FieldValue Language
dc.contributor.authorBergmann, Simoneen
dc.contributor.authorEichhorn, Ingaen
dc.contributor.authorKohler, Thomas Pen
dc.contributor.authorHammerschmidt, Svenen
dc.contributor.authorGoldmann, Oliveren
dc.contributor.authorRohde, Manfreden
dc.contributor.authorFulde, Marcusen
dc.date.accessioned2018-01-02T14:17:40Z-
dc.date.available2018-01-02T14:17:40Z-
dc.date.issued2017-
dc.identifier.citationSCM, the M Protein of Streptococcus canis Binds Immunoglobulin G. 2017, 7:80 Front Cell Infect Microbiolen
dc.identifier.issn2235-2988-
dc.identifier.pmid28401063-
dc.identifier.doi10.3389/fcimb.2017.00080-
dc.identifier.urihttp://hdl.handle.net/10033/621217-
dc.description.abstractThe M protein of Streptococcus canis (SCM) is a virulence factor and serves as a surface-associated receptor with a particular affinity for mini-plasminogen, a cleavage product of the broad-spectrum serine protease plasmin. Here, we report that SCM has an additional high-affinity immunoglobulin G (IgG) binding activity. The ability of a particular S. canis isolate to bind to IgG significantly correlates with a scm-positive phenotype, suggesting a dominant role of SCM as an IgG receptor. Subsequent heterologous expression of SCM in non-IgG binding S. gordonii and Western Blot analysis with purified recombinant SCM proteins confirmed its IgG receptor function. As expected for a zoonotic agent, the SCM-IgG interaction is species-unspecific, with a particular affinity of SCM for IgGs derived from human, cats, dogs, horses, mice, and rabbits, but not from cows and goats. Similar to other streptococcal IgG-binding proteins, the interaction between SCM and IgG occurs via the conserved Fc domain and is, therefore, non-opsonic. Interestingly, the interaction between SCM and IgG-Fc on the bacterial surface specifically prevents opsonization by C1q, which might constitute another anti-phagocytic mechanism of SCM. Extensive binding analyses with a variety of different truncated SCM fragments defined a region of 52 amino acids located in the central part of the mature SCM protein which is important for IgG binding. This binding region is highly conserved among SCM proteins derived from different S. canis isolates but differs significantly from IgG-Fc receptors of S. pyogenes and S. dysgalactiae sub. equisimilis, respectively. In summary, we present an additional role of SCM in the pathogen-host interaction of S. canis. The detailed analysis of the SCM-IgG interaction should contribute to a better understanding of the complex roles of M proteins in streptococcal pathogenesis.en
dc.language.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshAnimalsen
dc.subject.meshAntigen-Antibody Reactionsen
dc.subject.meshAntigens, Bacterialen
dc.subject.meshBacterial Outer Membrane Proteinsen
dc.subject.meshBacterial Proteinsen
dc.subject.meshCarrier Proteinsen
dc.subject.meshCatsen
dc.subject.meshCattleen
dc.subject.meshCloning, Molecularen
dc.subject.meshDogsen
dc.subject.meshGoatsen
dc.subject.meshHorsesen
dc.subject.meshHost-Pathogen Interactionsen
dc.subject.meshHumansen
dc.subject.meshImmunoglobulin Fc Fragmentsen
dc.subject.meshImmunoglobulin Gen
dc.subject.meshPhylogenyen
dc.subject.meshProtein Bindingen
dc.subject.meshRabbitsen
dc.subject.meshRecombinant Proteinsen
dc.subject.meshStreptococcusen
dc.subject.meshVirulence Factorsen
dc.subject.meshZoonosesen
dc.titleSCM, the M Protein of Streptococcus canis Binds Immunoglobulin G.en
dc.typeArticleen
dc.contributor.departmentHelmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr.7, 38124 Braunschweig, Germany.en
dc.identifier.journalFrontiers in cellular and infection microbiologyen

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