Journal
EMBO JOURNAL
Volume 19, Issue 7, Pages 1458-1466Publisher
WILEY
DOI: 10.1093/emboj/19.7.1458
Keywords
gC1q-R; InlB; invasion; Listeria; signaling
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InlB is a Listeria monocytogenes protein that promotes entry of the bacterium into mammalian cells by stimulating tyrosine phosphorylation of the adaptor proteins Gab1, Cb1 and Shc, and activation of phosphatidylinositol (PI) 3-kinase. Using affinity chromatography and enzyme-linked immunosorbent assay, we demonstrate a direct interaction between InlB and the mammalian protein gC1q-R, the receptor of the globular part of the complement component C1q, Soluble C1q or anti-gC1q-R antibodies impair InlB-mediated entry. Transient transfection of GPC16 cells, which are non-permissive to InlB-mediated entry, with a plasmid-expressing human gC1q-R promotes entry of InlB-coated beads. Furthermore, several experiments indicate that membrane recruitment and activation of PI 3-kinase involve an InlB-gC1q-R interaction and that gC1q-R associates with Gab1 upon stimulation of Vero cells with InlB, Thus, gC1q-R constitutes a cellular receptor involved in InlB-mediated activation of PI 3-kinase and tyrosine phosphorylation of the adaptor protein Gab1, After E-cadherin, the receptor for internalin, gC1q-R is the second identified mammalian receptor promoting entry of L.monocytogenes into mammalian cells.
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