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dc.contributor.authorFulde, Marcus
dc.contributor.authorRohde, Manfred
dc.contributor.authorPolok, Andy
dc.contributor.authorPreissner, Klaus T
dc.contributor.authorChhatwal, Gursharan Singh
dc.contributor.authorBergmann, Simone
dc.date.accessioned2013-09-03T09:42:19Z
dc.date.available2013-09-03T09:42:19Z
dc.date.issued2013
dc.identifier.citationCooperative plasminogen recruitment to the surface of Streptococcus canis via M protein and enolase enhances bacterial survival. 2013, 4 (2):e00629-12 MBioen_GB
dc.identifier.issn2150-7511
dc.identifier.pmid23481605
dc.identifier.doi10.1128/mBio.00629-12
dc.identifier.urihttp://hdl.handle.net/10033/300682
dc.description.abstractStreptococcus canis is a zoonotic pathogen capable of causing serious invasive diseases in domestic animals and humans. Surface-exposed M proteins and metabolic enzymes have been characterized as major virulence determinants in various streptococcal species. Recently, we have identified SCM, the M-like protein of S. canis, as the major receptor for miniplasminogen localized on the bacterial surface. The present study now characterizes the glycolytic enzyme enolase as an additional surface-exposed plasminogen-binding protein. According to its zoonotic properties, purified S. canis enolase binds to both human and canine plasminogen and facilitates degradation of aggregated fibrin matrices after activation with host-derived urokinase-type plasminogen activator (uPA). Unlike SCM, which binds to the C terminus of human plasminogen, the S. canis enolase interacts N terminally with the first four kringle domains of plasminogen, representing angiostatin. Radioactive binding analyses confirmed cooperative plasminogen recruitment to both surface-exposed enolase and SCM. Furthermore, despite the lack of surface protease activity via SpeB in S. canis, SCM is released and reassociated homophilically to surface-anchored SCM and heterophilically to surface-bound plasminogen. In addition to plasminogen-mediated antiphagocytic activity, reassociation of SCM to the bacterial surface significantly enhanced bacterial survival in phagocytosis analyses using human neutrophils.
dc.language.isoenen
dc.rightsArchived with thanks to mBioen_GB
dc.subject.meshAnimalsen_GB
dc.subject.meshAntigens, Bacterialen_GB
dc.subject.meshBacterial Outer Membrane Proteinsen_GB
dc.subject.meshCarrier Proteinsen_GB
dc.subject.meshHumansen_GB
dc.subject.meshMicrobial Viabilityen_GB
dc.subject.meshPhosphopyruvate Hydrataseen_GB
dc.subject.meshPlasminogenen_GB
dc.subject.meshProtein Bindingen_GB
dc.subject.meshStreptococcusen_GB
dc.titleCooperative plasminogen recruitment to the surface of Streptococcus canis via M protein and enolase enhances bacterial survival.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for Infection Research (HZI), Department of Medical Microbiology, Braunschweig, Germany. marcus.fulde@web.deen_GB
dc.identifier.journalmBioen_GB
refterms.dateFOA2018-06-13T03:56:08Z
html.description.abstractStreptococcus canis is a zoonotic pathogen capable of causing serious invasive diseases in domestic animals and humans. Surface-exposed M proteins and metabolic enzymes have been characterized as major virulence determinants in various streptococcal species. Recently, we have identified SCM, the M-like protein of S. canis, as the major receptor for miniplasminogen localized on the bacterial surface. The present study now characterizes the glycolytic enzyme enolase as an additional surface-exposed plasminogen-binding protein. According to its zoonotic properties, purified S. canis enolase binds to both human and canine plasminogen and facilitates degradation of aggregated fibrin matrices after activation with host-derived urokinase-type plasminogen activator (uPA). Unlike SCM, which binds to the C terminus of human plasminogen, the S. canis enolase interacts N terminally with the first four kringle domains of plasminogen, representing angiostatin. Radioactive binding analyses confirmed cooperative plasminogen recruitment to both surface-exposed enolase and SCM. Furthermore, despite the lack of surface protease activity via SpeB in S. canis, SCM is released and reassociated homophilically to surface-anchored SCM and heterophilically to surface-bound plasminogen. In addition to plasminogen-mediated antiphagocytic activity, reassociation of SCM to the bacterial surface significantly enhanced bacterial survival in phagocytosis analyses using human neutrophils.


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