Penicillin binding protein 3 of Staphylococcus aureus NCTC 8325-4 binds and activates human plasminogen
| Autor: | Veera Kainulainen, Riikka Kylväjä, Tuomas Ojalehto, Benita Westerlund-Wikström, Ritva Virkola |
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| Přispěvatelé: | Biosciences, Medicum, Department of Pharmacology, General Microbiology, Molecular Mechanisms of Bacteria in Infectious Diseases and Health |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Staphylococcus aureus Penicillin binding proteins Penicillin binding protein Plasmin 030106 microbiology Short Report Virulence Plasma protein binding Biology medicine.disease_cause General Biochemistry Genetics and Molecular Biology Microbiology law.invention 03 medical and health sciences Bacterial Proteins Staphylococcus aureus Penicillin binding protein Plasminogen Plasmin Adhesion law medicine Humans Penicillin-Binding Proteins Fibrinolysin Escherichia coli 1183 Plant biology microbiology virology Medicine(all) Biochemistry Genetics and Molecular Biology(all) Plasminogen General Medicine Recombinant Proteins 3. Good health Immobilized Proteins Solubility Recombinant DNA Adhesion 1182 Biochemistry cell and molecular biology Penicillin binding medicine.drug Protein Binding |
| Zdroj: | BMC Research Notes |
| Popis: | 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. Electronic supplementary material The online version of this article (doi:10.1186/s13104-016-2190-4) contains supplementary material, which is available to authorized users. |
| Databáze: | OpenAIRE |
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