Identification of differentially expressed proteins from Burkholderia pseudomallei isolated during primary and relapsing melioidosis

被引:8
|
作者
Velapatino, Billie [6 ]
Limmathurotsakul, Direk [4 ,5 ]
Peacock, Sharon J. [3 ,4 ]
Speert, David P. [1 ,2 ]
机构
[1] Univ British Columbia, Dept Pediat, Div Infect & Immunol Dis, Vancouver, BC V5Z 4H4, Canada
[2] British Columbia Childrens Hosp Vancouver, Ctr Understanding & Preventing Infect Children, Res Ctr, Vancouver, BC V5Z 4H4, Canada
[3] Univ Cambridge, Addenbrookes Hosp, Dept Med, Cambridge CB2 2QQ, England
[4] Mahidol Univ, Fac Trop Med, Mahidol Oxford Trop Med Res Unit, Bangkok 10400, Thailand
[5] Mahidol Univ, Fac Trop Med, Dept Trop Hyg, Bangkok 10400, Thailand
[6] Univ British Columbia, Dept Pathol & Lab Med, Vancouver, BC V5Z 4H4, Canada
基金
英国惠康基金; 加拿大健康研究院;
关键词
Burkholderia pseudomallei; iTRAQ; 2D-PAGE; Melioidosis; Proteomics; MYCOBACTERIUM-TUBERCULOSIS; VI-SECRETION; COLONY MORPHOLOGY; HUMAN MACROPHAGES; SURVIVAL; REQUIRES; LOCUS;
D O I
10.1016/j.micinf.2011.11.011
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Burkholderia pseudomallei causes septicemic melioidosis with a high rate of relapse, however microbial determinants of relapse are unknown. Proteins were analyzed from sequential B. pseudomallei isolates from primary and relapsing melioidosis. Analysis by isotope tagging for relative and absolute quantitation revealed that factors required for nitric oxide detoxification (HmpA) and necessary for anaerobic growth (ArcA, ArcC and ArcB) were highly expressed in the relapse isolate. Two-dimensional gel electrophoresis revealed up-regulation of a putative hemolysin-coregulated protein in the primary isolate, and flagellin and HSP20/alpha crystalline in the relapse isolate. These observations provide targets for further analysis of latency and virulence of melioidosis. (C) 2011 Institut Pasteur. Published by Elsevier Masson SAS. All rights reserved.
引用
收藏
页码:335 / 340
页数:6
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