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

doi:10.1128/JB.187.23.8172-8180.2005

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 journal › Article

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 language	English (US)
Pages (from-to)	8172-8180
Number of pages	9
Journal	Journal of Bacteriology
Volume	187
Issue number	23
DOIs	https://doi.org/10.1128/JB.187.23.8172-8180.2005
State	Published - Dec 2005
Externally published	Yes

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

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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.",

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

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AU - Choi, Megan W.

AU - Murphy, Gloria A.

AU - Gonzales, Arlene D.

AU - Corzett, Chris H.

AU - Chang, Brian C.

AU - Fitch, J. Patrick

AU - McCutchen-Maloney, Sandra L.

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