SCM, a novel M-like protein from Streptococcus canis, binds (mini)-plasminogen with high affinity and facilitates bacterial transmigration.

2.50
Hdl Handle:
http://hdl.handle.net/10033/138570
Title:
SCM, a novel M-like protein from Streptococcus canis, binds (mini)-plasminogen with high affinity and facilitates bacterial transmigration.
Authors:
Fulde, Marcus; Rohde, Manfred; Hitzmann, Angela; Preissner, Klaus T; Nitsche-Schmitz, D Patric; Nerlich, Andreas; Chhatwal, Gursharan Singh; Bergmann, Simone
Abstract:
Streptococcus canis is an important zoonotic pathogen capable of causing serious invasive diseases in domestic animals and humans. In the present paper we report the binding of human plasminogen to S. canis and the recruitment of proteolytically active plasmin on its surface. The binding receptor for plasminogen was identified as a novel M-like protein designated SCM (S. canis M-like protein). SPR (surface plasmon resonance) analyses, radioactive dot-blot analyses and heterologous expression on the surface of Streptococcus gordonii confirmed the plasminogen-binding capability of SCM. The binding domain was located within the N-terminus of SCM, which specifically bound to the C-terminal part of plasminogen (mini-plasminogen) comprising kringle domain 5 and the catalytic domain. In the presence of urokinase, SCM mediated plasminogen activation on the bacterial surface that was inhibited by serine protease inhibitors and lysine amino acid analogues. Surface-bound plasmin effectively degraded purified fibrinogen as well as fibrin clots, resulting in the dissolution of fibrin thrombi. Electron microscopic illustration and time-lapse imaging demonstrated bacterial transmigration through fibrinous thrombi. The present study has led, for the first time, to the identification of SCM as a novel receptor for (mini)-plasminogen mediating the fibrinolytic activity of S. canis.
Affiliation:
Department of Medical Microbiology, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany. Marcus.Fulde@helmholtz-hzi.de
Citation:
SCM, a novel M-like protein from Streptococcus canis, binds (mini)-plasminogen with high affinity and facilitates bacterial transmigration. 2011, 434 (3):523-35 Biochem. J.
Journal:
The Biochemical journal
Issue Date:
24-Feb-2011
URI:
http://hdl.handle.net/10033/138570
DOI:
10.1042/BJ20101121
PubMed ID:
21210764
Type:
Article
Language:
en
ISSN:
1470-8728
Appears in Collections:
Publications of Dept. Medizinische Mikrobiologie (MMIK)

Full metadata record

DC FieldValue Language
dc.contributor.authorFulde, Marcusen
dc.contributor.authorRohde, Manfreden
dc.contributor.authorHitzmann, Angelaen
dc.contributor.authorPreissner, Klaus Ten
dc.contributor.authorNitsche-Schmitz, D Patricen
dc.contributor.authorNerlich, Andreasen
dc.contributor.authorChhatwal, Gursharan Singhen
dc.contributor.authorBergmann, Simoneen
dc.date.accessioned2011-08-02T13:41:44Z-
dc.date.available2011-08-02T13:41:44Z-
dc.date.issued2011-02-24-
dc.identifier.citationSCM, a novel M-like protein from Streptococcus canis, binds (mini)-plasminogen with high affinity and facilitates bacterial transmigration. 2011, 434 (3):523-35 Biochem. J.en
dc.identifier.issn1470-8728-
dc.identifier.pmid21210764-
dc.identifier.doi10.1042/BJ20101121-
dc.identifier.urihttp://hdl.handle.net/10033/138570-
dc.description.abstractStreptococcus canis is an important zoonotic pathogen capable of causing serious invasive diseases in domestic animals and humans. In the present paper we report the binding of human plasminogen to S. canis and the recruitment of proteolytically active plasmin on its surface. The binding receptor for plasminogen was identified as a novel M-like protein designated SCM (S. canis M-like protein). SPR (surface plasmon resonance) analyses, radioactive dot-blot analyses and heterologous expression on the surface of Streptococcus gordonii confirmed the plasminogen-binding capability of SCM. The binding domain was located within the N-terminus of SCM, which specifically bound to the C-terminal part of plasminogen (mini-plasminogen) comprising kringle domain 5 and the catalytic domain. In the presence of urokinase, SCM mediated plasminogen activation on the bacterial surface that was inhibited by serine protease inhibitors and lysine amino acid analogues. Surface-bound plasmin effectively degraded purified fibrinogen as well as fibrin clots, resulting in the dissolution of fibrin thrombi. Electron microscopic illustration and time-lapse imaging demonstrated bacterial transmigration through fibrinous thrombi. The present study has led, for the first time, to the identification of SCM as a novel receptor for (mini)-plasminogen mediating the fibrinolytic activity of S. canis.en
dc.language.isoenen
dc.subject.meshAnimalsen
dc.subject.meshBacterial Proteinsen
dc.subject.meshBinding Sitesen
dc.subject.meshCarrier Proteinsen
dc.subject.meshCatalytic Domainen
dc.subject.meshCatsen
dc.subject.meshDogsen
dc.subject.meshFibrinen
dc.subject.meshFibrinogenen
dc.subject.meshFibrinolysinen
dc.subject.meshHost-Pathogen Interactionsen
dc.subject.meshHumansen
dc.subject.meshKringlesen
dc.subject.meshPlasmaen
dc.subject.meshPlasminogenen
dc.subject.meshProtein Bindingen
dc.subject.meshStreptococcusen
dc.subject.meshSwineen
dc.titleSCM, a novel M-like protein from Streptococcus canis, binds (mini)-plasminogen with high affinity and facilitates bacterial transmigration.en
dc.typeArticleen
dc.contributor.departmentDepartment of Medical Microbiology, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany. Marcus.Fulde@helmholtz-hzi.deen
dc.identifier.journalThe Biochemical journalen

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