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dc.contributor.authorBergmann, René
dc.contributor.authorDinkla, Katrin
dc.contributor.authorNitsche-Schmitz, D Patric
dc.contributor.authorGraham, Rikki M A
dc.contributor.authorLüttge, Melanie
dc.contributor.authorSanderson-Smith, Martina L
dc.contributor.authorNerlich, Andreas
dc.contributor.authorRohde, Manfred
dc.contributor.authorChhatwal, Gursharan S
dc.date.accessioned2011-08-15T09:10:24Zen
dc.date.available2011-08-15T09:10:24Zen
dc.date.issued2011-02en
dc.identifier.citationBiological functions of GCS3, a novel plasminogen-binding protein of Streptococcus dysgalactiae ssp. equisimilis. 2011, 301 (2):157-64 Int. J. Med. Microbiol.en
dc.identifier.issn1618-0607en
dc.identifier.pmid20951639en
dc.identifier.doi10.1016/j.ijmm.2010.06.007en
dc.identifier.urihttp://hdl.handle.net/10033/139689en
dc.description.abstractIncreasing awareness of the relevance of Streptococcus dysgalactiae ssp. equisimilis as a human pathogen motivates the analysis of its pathomechanisms. One of the mechanisms that increases infectivity and dissemination of several streptococcal species is the recruitment and subsequent activation of host plasminogen on the streptococcal surface. This study identified GCS3 as a novel plasminogen-binding M protein of S. dysgalactiae ssp. equisimilis and revealed a difference in the mode of binding as compared to the plasminogen-binding protein PAM of S. pyogenes. In contrast to PAM, GCS3 did not bind to the kringle 1-3 region of plasminogen. Despite this difference, GCS3 exerts the same function of recruiting plasminogen to the streptococcal surface, which can be activated by streptokinase and host plasminogen activators to serve as a spreading factor. Moreover, we demonstrate a role of GCS3 in plasminogen-dependent streptococcal adherence to human pharyngeal cells (cell line Detroit 562) that indicates an additional function of the protein as an adhesin in the oral cavity.
dc.language.isoenen
dc.subject.meshAdhesins, Bacterialen
dc.subject.meshBacterial Adhesionen
dc.subject.meshBacterial Proteinsen
dc.subject.meshCarrier Proteinsen
dc.subject.meshCell Lineen
dc.subject.meshEpithelial Cellsen
dc.subject.meshHumansen
dc.subject.meshPlasminogenen
dc.subject.meshStreptococcusen
dc.subject.meshVirulence Factorsen
dc.titleBiological functions of GCS3, a novel plasminogen-binding protein of Streptococcus dysgalactiae ssp. equisimilis.en
dc.typeArticleen
dc.contributor.departmentDept. of Medical Microbiology, Helmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Braunschweig, Germany.en
dc.identifier.journalInternational journal of medical microbiology : IJMMen
refterms.dateFOA2018-06-13T01:05:37Z
html.description.abstractIncreasing awareness of the relevance of Streptococcus dysgalactiae ssp. equisimilis as a human pathogen motivates the analysis of its pathomechanisms. One of the mechanisms that increases infectivity and dissemination of several streptococcal species is the recruitment and subsequent activation of host plasminogen on the streptococcal surface. This study identified GCS3 as a novel plasminogen-binding M protein of S. dysgalactiae ssp. equisimilis and revealed a difference in the mode of binding as compared to the plasminogen-binding protein PAM of S. pyogenes. In contrast to PAM, GCS3 did not bind to the kringle 1-3 region of plasminogen. Despite this difference, GCS3 exerts the same function of recruiting plasminogen to the streptococcal surface, which can be activated by streptokinase and host plasminogen activators to serve as a spreading factor. Moreover, we demonstrate a role of GCS3 in plasminogen-dependent streptococcal adherence to human pharyngeal cells (cell line Detroit 562) that indicates an additional function of the protein as an adhesin in the oral cavity.


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