Proteomic characterization of Yersinia pestis virulence

被引：57

作者：

Chromy, BA ^{[1
]}

Choi, MW ^{[1
]}

Murphy, GA ^{[1
]}

Gonzales, AD ^{[1
]}

Corzett, CH ^{[1
]}

Chang, BC ^{[1
]}

Fitch, JP ^{[1
]}

McCutchen-Maloney, SL ^{[1
]}

机构：

[1] Lawrence Livermore Natl Lab, Biosci Directorate, Livermore, CA 94550 USA

来源：

JOURNAL OF BACTERIOLOGY | 2005年 / 187卷 / 23期

关键词：

D O I：

10.1128/JB.187.23.8172-8180.2005

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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 (Cafl), 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.

引用

页码：8172 / 8180

页数：9

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