| Literature DB >> 21444667 |
Renate Kastner1, Olivier Dussurget, Cristel Archambaud, Elisabeth Kernbauer, Didier Soulat, Pascale Cossart, Thomas Decker.
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.Entities:
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Year: 2011 PMID: 21444667 PMCID: PMC3125854 DOI: 10.1128/IAI.05073-11
Source DB: PubMed Journal: Infect Immun ISSN: 0019-9567 Impact factor: 3.441