| Title |
Comparative Proteome Analysis of Bacillus anthracis with pXO1 Plasmid Content |
| Author |
Sudipto Shahid1, Ji Hyun Park1, Hyung Tae Lee1, Seong-Joo Kim1, Ji Cheon Kim1, Sang Hoon Kim1, Dal Mu Ri Han1, Dong In Jeon1, Kyoung Hwa Jung2, and Young Gyu Chai1* |
| Address |
1Division of Molecular and Life Sciences, Hanyang University, Ansan 426-791, Republic of Korea, 2Institute of Natural Science and Technology, Hanyang University, Ansan 426-791, Republic of Korea |
| Bibliography |
Journal of Microbiology, 48(6),771-777, 2010,
|
| DOI |
|
| Key Words |
B. anthracis, 2-DE, MALDI-TOF MS, virulence factor, pXO1 |
| Abstract |
Bacillus anthracis the causative agent of anthrax, is an important pathogen among the Bacillus cereus group of species because of its physiological characteristics and its importance as a biological warfare agent. Tripartite anthrax toxin proteins and a poly-D-glutamic acid capsule are produced by B. anthracis vegetative
cells during mammalian hosts infection and when cultured in conditions that are thought to mimic the host environment. To identify the factors regulating virulence in B. anthracis the whole cell proteins were extracted from two B. anthracis strains and separated by narrow range immobilized pH gradient (IPG) strips (pH 4-7),
followed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Proteins that were differentially expressed were identified by the peptide fingerprinting using matrix-assisted laser desorption ionization–time-of-flight mass spectrometry (MALDI-TOF MS). A total of 23 proteins were identified as
being either upregulated or downregulated in the presence or absence of the virulence plasmid pXO1. Two plasmid encoded proteins and 12 cellular proteins were identified and documented as potential virulence factors. |
