Laurence Braun
Pasteur Institute
11 Papers
158 Citations
Laurence Braun is an academic researcher from Pasteur Institute. The author has contributed to research in topics: Internalin & Biology. The author has an hindex of 10, co-authored 10 publications.
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Papers
gC1q-R/p32, a C1q-binding protein, is a receptor for the InlB invasion protein of Listeria monocytogenes.
TL;DR: GC1q‐R constitutes a cellular receptor involved in InlB‐mediated activation of PI 3‐kinase and tyrosine phosphorylation of the adaptor protein Gab1, the second identified mammalian receptor promoting entry of L.monocytogenes into mammalian cells.
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Internalin of Listeria monocytogenes with an Intact Leucine-Rich Repeat Region Is Sufficient To Promote Internalization
TL;DR: It is demonstrated for the first time that the internalin protein alone is sufficient to promote internalization into cells expressing its receptor and confers invasiveness to both Enterococcus faecalis and internalin-coated latex beads.
288
InlB: an invasion protein of Listeria monocytogenes with a novel type of surface association
TL;DR: It is demonstrated that the last 232 amino acids of InlB are both necessary and sufficient for anchoring this protein to the bacterial surface and a ‘domain‐swapping’ strategy resulted in a chimeric protein that was anchored to the cell surface and able to confer entry.
253
The InlB protein of Listeria monocytogenes is sufficient to promote entry into mammalian cells
TL;DR: Data indicate that InlB is sufficient for entry of L. monocytogenes into host cells and suggest that this protein is an effector of host cell signalling pathways.
189
The 213-amino-acid leucine-rich repeat region of the listeria monocytogenes InlB protein is sufficient for entry into mammalian cells, stimulation of PI 3-kinase and membrane ruffling.
TL;DR: Results show that the first 213 amino acids of InlB are critical for its specific properties, and that purified Inl B can stimulate PI 3‐kinase activity and is thus the first bacterial agonist of this lipid kinase.
102