Differential analysis of Bacillus anthracis after pX01 plasmid curing and comprehensive data on Bacillus anthracis infection in macrophages and glial cells

Sung Ha Park, Hee Bok Oh, Won Keun Seong, Chan Wha Kim, Sang Yun Cho, Cheon Kwon Yoo

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Bacillus anthracis is a gram-positive bacterial organism responsible for anthrax. This organism has two pathogenic plasmids: pX01 and pX02. The genetic function of pX01, which comprises about 198 kb, is not known, except for a region called the pathogenic island, which contains three genes - pag, lef. and cya - that code for three toxic proteins. A 2-D difference gel electrophoresis (2-D DIGE) system was used to verify the existence of proteins controlled by the pX01 plasmid, and protein regulation data were obtained using DeCyder software. A total of 1728 proteins were identified in the wild-type strain of this organism and 1684 in the pX01 plasmid. Twenty-seven of these proteins disappeared and eight appeared when the pX01 plasmid was removed. An additional 52 proteins were downregulated and 15 were upregulated when this plasmid was removed. A total of 102 proteins have been identified using the MALDI-TOF method of analysis, including 49 whose functions are unknown. Among these, 31 participate in metabolic processes, two in cellular processes, 15 in the processing of genetic information, and five in the processing of extracellular information. Another seven proteins participate in bacterial virulence and pathogenesis. We investigated the functions of these proteins in other bacteria, particularly the B. anthracis derivative H9041. Bacterial growth differed between pX01+/pX02+ B. anthracis and its pX01-/pX02+ derivative as did the cytotoxicity of macrophages infected by pX01+/pX02+ B. anthracis and the pX01-pX02+ derivative. We also found that S100B protein levels increased in the host infected with pX01+/pX02+ B. anthratis or its pX01-/pX02+ derivative. These data suggest that the pX01 plasmid plays a key role in the regulation of protein functions in B. anthracis.

Original languageEnglish
Pages (from-to)3743-3758
Number of pages16
JournalProteomics
Volume7
Issue number20
DOIs
Publication statusPublished - 2007 Oct 1

Fingerprint

Bacillus anthracis
Macrophages
Bacilli
Neuroglia
Curing
Plasmids
Infection
Proteins
Derivatives
Automatic Data Processing
Anthrax
Poisons
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Electrophoresis, Gel, Two-Dimensional
Cytotoxicity
Processing
Electrophoresis
Islands
Virulence
Bacteria

Keywords

  • B. anthracis
  • Matrix-assisted laser desorption/ionization time of flight mass spectrometry
  • pX01 plasmid
  • Two-dimensional difference gel electrophoresis

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Differential analysis of Bacillus anthracis after pX01 plasmid curing and comprehensive data on Bacillus anthracis infection in macrophages and glial cells. / Park, Sung Ha; Oh, Hee Bok; Seong, Won Keun; Kim, Chan Wha; Cho, Sang Yun; Yoo, Cheon Kwon.

In: Proteomics, Vol. 7, No. 20, 01.10.2007, p. 3743-3758.

Research output: Contribution to journalArticle

Park, Sung Ha ; Oh, Hee Bok ; Seong, Won Keun ; Kim, Chan Wha ; Cho, Sang Yun ; Yoo, Cheon Kwon. / Differential analysis of Bacillus anthracis after pX01 plasmid curing and comprehensive data on Bacillus anthracis infection in macrophages and glial cells. In: Proteomics. 2007 ; Vol. 7, No. 20. pp. 3743-3758.
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AU - Cho, Sang Yun

AU - Yoo, Cheon Kwon

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AB - Bacillus anthracis is a gram-positive bacterial organism responsible for anthrax. This organism has two pathogenic plasmids: pX01 and pX02. The genetic function of pX01, which comprises about 198 kb, is not known, except for a region called the pathogenic island, which contains three genes - pag, lef. and cya - that code for three toxic proteins. A 2-D difference gel electrophoresis (2-D DIGE) system was used to verify the existence of proteins controlled by the pX01 plasmid, and protein regulation data were obtained using DeCyder software. A total of 1728 proteins were identified in the wild-type strain of this organism and 1684 in the pX01 plasmid. Twenty-seven of these proteins disappeared and eight appeared when the pX01 plasmid was removed. An additional 52 proteins were downregulated and 15 were upregulated when this plasmid was removed. A total of 102 proteins have been identified using the MALDI-TOF method of analysis, including 49 whose functions are unknown. Among these, 31 participate in metabolic processes, two in cellular processes, 15 in the processing of genetic information, and five in the processing of extracellular information. Another seven proteins participate in bacterial virulence and pathogenesis. We investigated the functions of these proteins in other bacteria, particularly the B. anthracis derivative H9041. Bacterial growth differed between pX01+/pX02+ B. anthracis and its pX01-/pX02+ derivative as did the cytotoxicity of macrophages infected by pX01+/pX02+ B. anthracis and the pX01-pX02+ derivative. We also found that S100B protein levels increased in the host infected with pX01+/pX02+ B. anthratis or its pX01-/pX02+ derivative. These data suggest that the pX01 plasmid plays a key role in the regulation of protein functions in B. anthracis.

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