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© Pierre Gounon
Entrée de Listeria dans une cellule épithéliale (Grossissement X 10000). Image colorisée.
Publication : Cellular microbiology

The invasion protein InIB from Listeria monocytogenes activates PLC-gamma1 downstream from PI 3-kinase

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Cellular microbiology - 01 Dec 2000

Bierne H, Dramsi S, Gratacap MP, Randriamampita C, Carpenter G, Payrastre B, Cossart P

Link to Pubmed [PMID] – 11207601

Cell. Microbiol. 2000 Dec;2(6):465-76

Entry of the bacterial pathogen Listeria monocytogenes into non-phagocytic mammalian cells is mainly mediated by the InlB protein. Here we show that in the human epithelial cell line HEp-2, the invasion protein InlB activates sequentially a p85beta-p110 class I(A) PI 3-kinase and the phospholipase C-gamma1 (PLC-gamma1) without detectable tyrosine phosphorylation of PLC-gamma1. Purified InlB stimulates association of PLC-gamma1 with one or more tyrosine-phosphorylated proteins, followed by a transient increase in intracellular inositol 1,4,5-trisphosphate (IP3) levels and a release of intracellular Ca2+ in a PI 3-kinase-dependent manner. Infection of HEp-2 cells with wild-type L. monocytogenes bacteria also induces association of PLC-gamma1 with phosphotyrosyl proteins. This interaction is undetectable upon infection with a deltainlB mutant revealing an InlB specific signal. Interestingly, pharmacological or genetic inactivation of PLC-gamma1 does not significantly affect InlB-mediated bacterial uptake, suggesting that InlB-mediated PLC-gamma1 activation and calcium mobilization are involved in post-internalization steps.

http://www.ncbi.nlm.nih.gov/pubmed/11207601