Proteomic characterization of Yersinia pestis virulence

Brett A. Chromy, Megan W. Choi, Gloria A. Murphy, Arlene D. Gonzales, Chris H. Corzett, Brian C. Chang, J. Patrick Fitch, Sandra L. McCutchen-Maloney

Research output: Contribution to journalArticle

60 Scopus citations

Abstract

The Yersinia pestis proteome was studied as a function of temperature and calcium by two-dimensional differential gel electrophoresis. Over 4,100 individual protein spots were detected, of which hundreds were differentially expressed. A total of 43 differentially expressed protein spots, representing 24 unique proteins, were identified by mass spectrometry. Differences in expression were observed for several virulence-associated factors, including catalase-peroxidase (KatY), murine toxin (Ymt), plasminogen activator (Pla), and F1 capsule antigen (Caf1), as well as several putative virulence factors and membrane-bound and metabolic proteins. Differentially expressed proteins not previously reported to contribute to virulence are candidates for more detailed mechanistic studies, representing potential new virulence determinants.

Original languageEnglish (US)
Pages (from-to)8172-8180
Number of pages9
JournalJournal of Bacteriology
Volume187
Issue number23
DOIs
StatePublished - Dec 2005
Externally publishedYes

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

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    Chromy, B. A., Choi, M. W., Murphy, G. A., Gonzales, A. D., Corzett, C. H., Chang, B. C., Fitch, J. P., & McCutchen-Maloney, S. L. (2005). Proteomic characterization of Yersinia pestis virulence. Journal of Bacteriology, 187(23), 8172-8180. https://doi.org/10.1128/JB.187.23.8172-8180.2005