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Infection and Immunity, December 2006, p. 6540-6546, Vol. 74, No. 12
0019-9567/06/$08.00+0 doi:10.1128/IAI.01106-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Department of Medicine, Division of Infectious Diseases, University of British Columbia, Vancouver, British Columbia, Canada
Received 14 July 2006/ Returned for modification 2 September 2006/ Accepted 5 September 2006
Adaptive gene expression in prokaryotes is mediated by protein kinases and phosphatases. These regulatory proteins mediate phosphorylation of histidine or aspartate in two-component systems and serine/threonine or tyrosine in eukaryotic and eukaryote-like protein kinase systems. The genome sequence of Mycobacterium avium subsp. paratuberculosis, the causative agent of Johne's disease, does not possess a defined tyrosine kinase. Nevertheless, it encodes for protein tyrosine phosphatases. Here, we report that Map1985, is a functional low-molecular tyrosine phosphatase that is secreted intracellularly upon macrophage infection. This finding suggests that Map1985 might contribute to the pathogenesis of Mycobacterium avium subsp. paratuberculosis by dephosphorylating essential macrophage signaling and/or adaptor molecules.
Published ahead of print on 18 September 2006.
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