期刊
CELLULAR MICROBIOLOGY
卷 13, 期 1, 页码 47-61出版社
WILEY
DOI: 10.1111/j.1462-5822.2010.01516.x
关键词
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资金
- NIH [R01 AI41440, R01 AI064285, R03 AI080993-01A1]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI032947, R01AI064285, R03AI080993, R01AI041440] Funding Source: NIH RePORTER
P>Anaplasma phagocytophilum causes human granulocytic anaplasmosis, one of the most common tick-borne diseases in North America. This unusual obligate intracellular pathogen selectively persists within polymorphonuclear leucocytes. In this study, using the yeast surrogate model we identified an A. phagocytophilum virulence protein, AptA (A. phagocytophilum toxin A), that activates mammalian Erk1/2 mitogen-activated protein kinase. This activation is important for A. phagocytophilum survival within human neutrophils. AptA interacts with the intermediate filament protein vimentin, which is essential for A. phagocytophilum-induced Erk1/2 activation and infection. A. phagocytophilum infection reorganizes vimentin around the bacterial inclusion, thereby contributing to intracellular survival. These observations reveal a major role for the bacterial protein, AptA, and the host protein, vimentin, in the activation of Erk1/2 during A. phagocytophilum infection.
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