Adhesion and Virulence Properties of Epidemic Canadian Methicillin‐ResistantStaphylococcus aureusStrain 1: Identification of Novel Adhesion Functions Associated with Plasmin‐Sensitive Surface Protein
Author(s) -
Mario Huesca,
Robert Peralta,
Daniel N. Sauder,
Andrew E. Simor,
Martin J. McGavin
Publication year - 2002
Publication title -
the journal of infectious diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.69
H-Index - 252
eISSN - 1537-6613
pISSN - 0022-1899
DOI - 10.1086/340123
Subject(s) - virulence , microbiology and biotechnology , plasmin , staphylococcus aureus , biology , glycolipid , extracellular matrix , strain (injury) , phenotype , extracellular , virulence factor , adhesion , bacteria , chemistry , genetics , gene , biochemistry , enzyme , organic chemistry , anatomy
Epidemic Canadian methicillin-resistant Staphylococcus aureus strain 1 (CMRSA-1) comprises related subtypes that differ in phenotype and prevalence, with subtypes 1A, 1B, and 1D representing 1%, 71%, and 18%, respectively, of total CMRSA-1 isolates. The predominant CMRSA-1B subtype possesses a variant of the staphylococcal cassette chromosome mec, harboring pls, which encodes plasmin-sensitive surface protein (Pls). CMRSA-1B cells that express Pls exhibited poor adhesion to keratinocyte extracellular matrix. However, CMRSA-1B and purified Pls adhered to cellular lipids and glycolipids, and Pls promoted bacterial cell-cell interactions. Although exoprotein expression was restricted to a precursor form of lipase in CMRSA-1B, it was not attenuated in virulence relative to CMRSA-1A, which exhibits normal exoprotein expression. In contrast, CMRSA-1D exhibited a pleiotropic defect in exoprotein expression and attenuated virulence relative to CMRSA-1A. These data indicate that the high transmissibility of CMRSA-1B was not achieved at the expense of attenuated virulence and that Pls confers a novel adhesion mechanism.
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