Dynamic proteome changes of Shigella flexneri 2a during transition from exponential growth to stationary phase.
- Author:
Li ZHU
1
;
Xian-Kai LIU
;
Ge ZHAO
;
Yi-Dan ZHI
;
Xin BU
;
Tian-Yi YING
;
Er-Ling FENG
;
Jie WANG
;
Xue-Min ZHANG
;
Pei-Tang HUANG
;
Heng-Liang WANG
Author Information
1. State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Biotechnology, Beijing 100071, China.
- Publication Type:Journal Article
- MeSH:
Bacterial Proteins;
analysis;
Computational Biology;
Electrophoresis, Gel, Two-Dimensional;
Gene Expression Profiling;
methods;
Kinetics;
Peptide Mapping;
Proteome;
analysis;
Proteomics;
methods;
Shigella flexneri;
growth & development;
metabolism;
pathogenicity;
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization;
Temperature;
Trypsin;
pharmacology;
Virulence
- From:
Genomics, Proteomics & Bioinformatics
2007;5(2):111-120
- CountryChina
- Language:English
-
Abstract:
Shigella flexneri is an infectious pathogen that causes dysentery to human, which remains a serious threat to public health, particularly in developing countries. In this study, the global protein expression patterns of S. flexneri during transition from exponential growth to stationary phase in vitro were analyzed by using 2-D PAGE combined with MALDI-TOF MS. In a time-course experiment with five time points, the relative abundance of 49 protein spots varied significantly. Interestingly, a putative outer membrane protein YciD (OmpW) was almost not detected in the exponential growth phase but became one of the most abundant proteins in the whole stationary-phase proteome. Some proteins regulated by the global regulator FNR were also significantly induced (such as AnsB, AspA, FrdAB, and KatG) or repressed (such as AceEF, OmpX, SodA, and SucAB) during the growth phase transition. These proteins may be the key effectors of the bacterial cell cycle or play important roles in the cellular maintenance and stress responses. Our expression profile data provide valuable information for the study of bacterial physiology and form the basis for future proteomic analyses of this pathogen.
