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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<jats:named-content content-type=\"genus-species\">S. canis<\/jats:named-content>, 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<jats:named-content content-type=\"genus-species\">S. canis<\/jats:named-content>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<jats:named-content content-type=\"genus-species\">S. canis<\/jats:named-content>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<jats:named-content content-type=\"genus-species\">S. canis<\/jats:named-content>, 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.<\/jats:p><jats:p><jats:bold>IMPORTANCE<\/jats:bold>Streptococcal infections are a major issue in medical microbiology due to the increasing spread of antibiotic resistances and the limited availability of efficient vaccines. Surface-exposed glycolytic enzymes and M proteins have been characterized as major virulence factors mediating pathogen-host interaction. Since streptococcal infection mechanisms exert a subset of multicombinatorial processes, the investigation of synergistic activities mediated via different virulence factors has become a high priority. Our data clearly demonstrate that plasminogen recruitment to the<jats:named-content content-type=\"genus-species\">Streptococcus canis<\/jats:named-content>surface via SCM and enolase in combination with SCM reassociation enhances bacterial survival by protecting against phagocytic killing. These data propose a new cooperative mechanism for prevention of phagocytic killing based on the synergistic activity of homophilic and heterophilic SCM binding in the presence of human plasminogen.<\/jats:p>","DOI":"10.1128\/mbio.00629-12","type":"journal-article","created":{"date-parts":[[2013,3,13]],"date-time":"2013-03-13T03:31:48Z","timestamp":1363145508000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":37,"title":["Cooperative Plasminogen Recruitment to the Surface of Streptococcus canis via M Protein and Enolase Enhances Bacterial Survival"],"prefix":"10.1128","volume":"4","author":[{"given":"Marcus","family":"Fulde","sequence":"first","affiliation":[{"name":"Helmholtz Centre for Infection Research (HZI), Department of Medical Microbiology, Braunschweig, Germany"},{"name":"Hannover Medical School, Institute for Medical Microbiology and Hospital Epidemiology, Hannover, 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