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LipA, a tyrosine and lipid phosphatase involved in the virulence of Listeria monocytogenes.


ABSTRACT: Intracellular bacterial pathogens manipulate host cell functions by producing enzymes that stimulate or antagonize signal transduction. The Listeria monocytogenes genome contains a gene, lmo1800, encoding a protein with a conserved motif of conventional tyrosine phosphatases. Here, we report that the lmo1800-encoded protein LipA is secreted by Listeria and displays tyrosine as well as lipid phosphatase activity in vitro. Bacteria lacking LipA are severely attenuated in virulence in vivo, thus revealing a so-far-undescribed enzymatic activity involved in Listeria infection.

SUBMITTER: Kastner R 

PROVIDER: S-EPMC3125854 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

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LipA, a tyrosine and lipid phosphatase involved in the virulence of Listeria monocytogenes.

Kastner Renate R   Dussurget Olivier O   Archambaud Cristel C   Kernbauer Elisabeth E   Soulat Didier D   Cossart Pascale P   Decker Thomas T  

Infection and immunity 20110328 6


Intracellular bacterial pathogens manipulate host cell functions by producing enzymes that stimulate or antagonize signal transduction. The Listeria monocytogenes genome contains a gene, lmo1800, encoding a protein with a conserved motif of conventional tyrosine phosphatases. Here, we report that the lmo1800-encoded protein LipA is secreted by Listeria and displays tyrosine as well as lipid phosphatase activity in vitro. Bacteria lacking LipA are severely attenuated in virulence in vivo, thus re  ...[more]

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