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KMID : 0880220100480060771
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Journal of Microbiology
2010 Volume.48 No. 6 p.771 ~ p.777
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Comparative proteome analysis of Bacillus anthracis with pXO1 plasmid content
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Sudipto Shahid
Park Ji-Hyun
Lee Hyung-Tae
Kim Seong-Joo
Kim Ji-Cheon
Kim Sang-Hoon
Han Dal-Mu-Ri
Jeon Dong-In
Jung Kyoung-Hwa
Chai Young-Gyu
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Abstract
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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.
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KEYWORD
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B. anthracis, 2-DE, MALDI-TOF MS, virulence factor, pXO1
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