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Microbiol Res. 2013 Oct 1;168(8):504-11. doi: 10.1016/j.micres.2013.03.004. Epub 2013 Apr 6.

Two dimensional electrophoresis of the exo-proteome produced from community acquired methicillin resistant Staphylococcus aureus belonging to clonal complex 80.

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  • 1Department of Structural Pathology, Graduate School of Medical and Dental Sciences, Niigata University, Niigata, Japan. shymaa21@yahoo.com

Abstract

Two-dimensional electrophoresis (2DE) combined with mass spectrometry was used to characterize the exo-proteome secreted by two strains (ER13 and ER21) representing community acquired methicillin resistant Staphylococcus aureus (CA-MRSA) belonging to clonal complex 80 (CC80). Common spots were detected between the 2 gels using the Progenesis SameSpots software. Two hundred and fifty-one and 312 spots from the exo-proteome of ER13 and ER21 were resolved, respectively. 2DE overlap comparison showed that 59 spots were shared. LC-MS/MS analysis identified 57 proteins from these spots comprising about 21% extracellular, 48% cytoplasmic, 2% cytoplasmic membrane, 2% cell wall, and 26% with unknown localization. The identified proteins were classified with respect to their Gene Ontology (GO) annotation as ∼24% virulence determinants and toxins, ∼17% involved in carbohydrate metabolism, ∼14% involved in environmental stress, and ∼12% associated with cell division. The identification of the enterotoxin B from the exo-products of both strains used in our study, as belonging to CC80 was interesting.

Copyright © 2013 Elsevier GmbH. All rights reserved.

KEYWORDS:

2DE; CA-MRSA; Exo-proteome; LC–MS/MS

PMID:
23566758
[PubMed - indexed for MEDLINE]
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