Penicillin binding protein 3 of Staphylococcus aureus NCTC 8325-4 binds and activates human plasminogen.

Show simple item record Kylväjä, Sanna Riikka Karoliina Ojalehto, Tuomas Heikki Ilari Kainulainen, Veera Liisa Virkola, Ritva Tuula Hannele Westerlund-Wikström, Benita Alice 2017-02-03T13:44:01Z 2017-02-03T13:44:01Z 2016-08-04
dc.identifier.citation Kylväjä , S R K , Ojalehto , T H I , Kainulainen , V L , Virkola , R T H & Westerlund-Wikström , B A 2016 , ' Penicillin binding protein 3 of Staphylococcus aureus NCTC 8325-4 binds and activates human plasminogen. ' , BMC research notes , vol. 9 , 389 .
dc.identifier.other PURE: 68953698
dc.identifier.other PURE UUID: 47b9e97a-6ca4-4d45-8061-6f22ed202517
dc.identifier.other Scopus: 84984996816
dc.identifier.other ORCID: /0000-0002-5307-3858/work/30075482
dc.description.abstract Background Staphylococcus aureus is a versatile pathogen expressing a number of virulence-associated adhesive molecules. In a previous study, we generated in a secretion-competent Escherichia coli strain a library of random FLAG-tag positive (FTP) polypeptides of S. aureus. To identify adhesive proteins and gain additional knowledge on putative virulence factors of S. aureus, we here screened the FTP library against human serum proteins. Findings Staphylococcus aureus NCTC 8325-4, origin of the FTP library, adhered to immobilized plasminogen in vitro. In an enzyme-linked immunoassay a C-terminal part of penicillin binding protein 3 (PBP3), included in the FTP library, bound to immobilized plasminogen. We expressed and purified full-length PBP3 and its C-terminal fragments as recombinant proteins. In a time-resolved fluorometry—based assay the PBP3 polypeptides bound to immobilized plasminogen. The polypeptides enhanced formation of plasmin from plasminogen as analyzed by cleavage of a chromogenic plasmin substrate. Conclusions The present findings, although preliminary, demonstrate reliably that S. aureus NCTC 8325-4 adheres to immobilized plasminogen in vitro and that the adhesion may be mediated by a C-terminal fragment of the PBP3 protein. The full length PBP3 and the penicillin binding C-terminal domain of PBP3 expressed as recombinant proteins bound plasminogen and activated plasminogen to plasmin. These phenomena were inhibited by the lysine analogue ε-aminocaproic acid suggesting that the binding is mediated by lysine residues. A detailed molecular description of surface molecules enhancing the virulence of S. aureus will aid in understanding of its pathogenicity and help in design of antibacterial drugs in the future en
dc.format.extent 10
dc.language.iso eng
dc.relation.ispartof BMC research notes
dc.rights cc_by
dc.rights.uri info:eu-repo/semantics/openAccess
dc.subject 1183 Plant biology, microbiology, virology
dc.subject Staphylococcus aureus, Penicillin binding protein, Plasminogen, Plasmin, Adhesion
dc.subject 1182 Biochemistry, cell and molecular biology
dc.title Penicillin binding protein 3 of Staphylococcus aureus NCTC 8325-4 binds and activates human plasminogen. en
dc.type Article
dc.contributor.organization Biosciences
dc.contributor.organization Medicum
dc.contributor.organization Department of Pharmacology
dc.contributor.organization General Microbiology
dc.contributor.organization Molecular Mechanisms of Bacteria in Infectious Diseases and Health
dc.description.reviewstatus Peer reviewed
dc.relation.issn 1756-0500
dc.rights.accesslevel openAccess
dc.type.version publishedVersion

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