Open AccessAnaplasma phagocytophilum AptA modulates Erk1/2 signalling
Author(s) -
Sukumaran Bindu,
Mastronunzio Juliana E.,
Narasimhan Sukanya,
Fankhauser Sarah,
Uchil Pradeep D.,
Levy Roie,
Graham Morven,
Colpitts Tonya Michelle,
Lesser Cammie F.,
Fikrig Erol
Publication year - 2011
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/j.1462-5822.2010.01516.x
Subject(s) - anaplasma phagocytophilum , biology , vimentin , virology , intracellular , microbiology and biotechnology , intracellular parasite , immunology , borrelia burgdorferi , immunohistochemistry , antibody
Summary 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.