期刊
MICROBIAL PATHOGENESIS
卷 47, 期 4, 页码 231-236出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.micpath.2009.08.002
关键词
Helicobacter pylori; Heat shock proteins
资金
- Public Health Service [AI42081]
- Mary and Floyd Schwall Fellowship at the University of California, Davis
Heat shock proteins (HSPs) are primarily known as molecular chaperones that are induced by cell stress and prevent protein aggregation and facilitate folding. Recent evidence suggests that exposure of cells to microbial pathogens can also induce HSPs, which then modulate both innate and adaptive immune responses. Paradoxically, Helicobacter pylori has been found to decrease expression of HSPs. We sought to investigate this phenomenon further and to examine the role of different H. pylori strains and recognized virulence factors in cell culture and in the mouse model. Co-culture of H. pylori with two gastric carcinoma cell lines reduced expression of HSP70 and, to a lesser extent, HSP60. Down modulation of HSPs was not dependent on the presence of the vacuolating cytotoxin (VacA) or the cag pathogenicity island (cag PAI). C57BL/6 mice infected with a human H. pylori strain also demonstrated reduced expression of HSP70, HSP8, and heat shock factor 1 (HSF-1),a transcriptional activator of HSP70. In contrast, the bacterial pathogen, S. Typhimurium up-regulated HSP expression. Since HSPs are thought to function as danger signals during microbial infection, H. pylori down-regulation of HSPs may be a mechanism of immune evasion that promotes chronic infection. (C) 2009 Published by Elsevier Ltd.
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