| Autor: |
Salazar N; Centro de Ciências Naturais e Humanas, Universidade Federal do ABCSanto André, Brazil., Castiblanco-Valencia MM; Departamento de Imunologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil., da Silva LB; Laboratório de Bacteriologia, Instituto Butantan, São Paulo, Brazil., de Castro Í; Departamento de Imunologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil., Monaris D; Laboratório de Bacteriologia, Instituto Butantan, São Paulo, Brazil., Masuda HP; Centro de Ciências Naturais e Humanas, Universidade Federal do ABCSanto André, Brazil., Barbosa AS; Laboratório de Bacteriologia, Instituto Butantan, São Paulo, Brazil., Arêas AP; Centro de Ciências Naturais e Humanas, Universidade Federal do ABCSanto André, Brazil. |
| Jazyk: |
angličtina |
| Zdroj: |
PloS one [PLoS One] 2014 Nov 19; Vol. 9 (11), pp. e112730. Date of Electronic Publication: 2014 Nov 19 (Print Publication: 2014). |
| DOI: |
10.1371/journal.pone.0112730 |
| Abstrakt: |
Infections caused by Staphylococcus aureus--particularly nosocomial infections--represent a great concern. Usually, the early stage of pathogenesis consists on asymptomatic nasopharynx colonization, which could result in dissemination to other mucosal niches or invasion of sterile sites, such as blood. This pathogenic route depends on scavenging of nutrients as well as binding to and disrupting extracellular matrix (ECM). Manganese transport protein C (MntC), a conserved manganese-binding protein, takes part in this infectious scenario as an ion-scavenging factor and surprisingly as an ECM and coagulation cascade binding protein, as revealed in this work. This study showed a marked ability of MntC to bind to several ECM and coagulation cascade components, including laminin, collagen type IV, cellular and plasma fibronectin, plasminogen and fibrinogen by ELISA. The MntC binding to plasminogen appears to be related to the presence of surface-exposed lysines, since previous incubation with an analogue of lysine residue, ε-aminocaproic acid, or increasing ionic strength affected the interaction between MntC and plasminogen. MntC-bound plasminogen was converted to active plasmin in the presence of urokinase plasminogen activator (uPA). The newly released plasmin, in turn, acted in the cleavage of the α and β chains of fibrinogen. In conclusion, we describe a novel function for MntC that may help staphylococcal mucosal colonization and establishment of invasive disease, through the interaction with ECM and coagulation cascade host proteins. These data suggest that this potential virulence factor could be an adequate candidate to compose an anti-staphylococcal human vaccine formulation. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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