Advanced search
Start date
Betweenand
Related content
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Staphylococcus aureus Manganese Transport Protein C (MntC) Is an Extracellular Matrix- and Plasminogen-Binding Protein

Full text
Author(s):
Salazar, Natalia [1] ; Castiblanco-Valencia, Monica Marcela [2] ; da Silva, Ludmila Bezerra [3] ; de Castro, Iris Arantes [2] ; Monaris, Denize [3] ; Masuda, Hana Paula [1] ; Barbosa, Angela Silva [3] ; Mattos Areas, Ana Paula [1]
Total Authors: 8
Affiliation:
[1] Univ Fed ABCSanto Andre, Ctr Ciencias Nat & Humanas, Santo Andre, SP - Brazil
[2] Univ Sao Paulo, Inst Ciencias Biomed, Dept Imunol, BR-05508 Sao Paulo - Brazil
[3] Inst Butantan, Bacteriol Lab, Sao Paulo - Brazil
Total Affiliations: 3
Document type: Journal article
Source: PLoS One; v. 9, n. 11 NOV 19 2014.
Web of Science Citations: 15
Abstract

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 surfaceexposed lysines, since previous incubation with an analogue of lysine residue, epsilon-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 alpha and beta 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. (AU)

FAPESP's process: 11/07297-3 - Colonization and evasion of host complement system by Leptospira: I. Functional characterization of the Elongation Factor Tu (EF-Tu) II. Interaction with human vitronectin
Grantee:Angela Silva Barbosa
Support Opportunities: Regular Research Grants
FAPESP's process: 10/50043-0 - Complement system and pathogenicity of Leptospires: mechanisms of activation and evasion, identification of bacterial ligands, characterization of proteases and establishment of an in vivo murine model
Grantee:Lourdes Isaac
Support Opportunities: Research Projects - Thematic Grants