Preliminary analysis on the proteomic feature of Guillain-Barré syndrome-associated Campylobacter jejuni

Autor(es): Tian Xin-ying,Zhang Jian-zhong,Li Chun-yan,He Li-hua,Liu Rui-chun,Yin Yan,Zou Qing-hua,Zhao Zhe

Resumo: To search the marker proteins of Guillain-Barré syndrome (GBS)-associated Campylobacter jejuni (C. jejuni) by comparing the protein maps of GBS-associated C. jejuni strains with that of non-GBS-associated C. jejuni strains. The whole-cell proteins of eight GBS-associated and eight non-GBS-associated C. jejuni strains were separated using the two-dimensional gel electrophoresis respectively. The differentially expressed proteins between the two sets of strains were identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF-MS) after in-gel tryptic digestion. Twenty differentially expressed spots were found with seventeen identified ones using MSCOT database. These proteins were identified as wlaX protein and some other proteins involving in energy metabolism (malate dehydrogenase, triosephosphate isomerase, Ni/Fe-hydrogenase small chain, cysteine synthase, branched-chain amino acid aminotransferase), cell process (heat shock protein, iron-uptake ABC transport system periplasmic iron-binding protein, alkyl hydroperoxide reductase), cell envelope (flagellin, UDP-N-acetylenolpyruvoylglucosamine reductase) etc. WlaX proteins were probably associated with LPS biosynthesis or virulence of C. jejuni. WlaX protein and flagellin protein were the possible marker-proteins of GBS-associated C. jejuni strains.

Palavras-Chave: Síndrome de Gilan-Barre ; Campylobacter jejuni ; eletroforese bidimensional

Imprenta: Zhonghua Liu Xing Bing Xue Za Zhi = Zhonghua Liuxingbingxue zazhi, v. 25, n. 3, p. 240-244, 2004

Descritores: Guillain-Barre Syndrome - Biosynthesis ; Guillain-Barre Syndrome - Biochemistry ; Guillain-Barre Syndrome - Cell ; Guillain-Barre Syndrome - Pathogenesis ; Guillain-Barre Syndrome - Protein synthesis ; Guillain-Barre Syndrome - Proteins

Data de publicação: 2004