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| Subject Categories: Membranes & Transport | Microbiology & Pathogens |
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| The EMBO Journal
(2002) 21, 5623–5634, doi: 10.1093/emboj/cdf558 |
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| GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands |
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| Michael Marino1, Manidipa Banerjee1, Renaud Jonquières2, Pascale Cossart2 and Partho Ghosh1 |
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1 Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0314, USA 2 Institut Pasteur, Unité des Interactions Bactéries−Cellules, 28 rue du Dr Roux, 75015 Paris, France To whom correspondence should be addressed Partho Ghosh, pghosh@ucsd.edu Received 11 July 2002; Revised 2 September 2002; Accepted 3 September 2002. |
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| Abstract |
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| InlB, a surface-localized protein of Listeria monocytogenes, induces phagocytosis in non-phagocytic mammalian cells by activating Met, a receptor tyrosine kinase. InlB also binds glycosaminoglycans and the protein gC1q-R, two additional host ligands implicated in invasion. We present the structure of InlB, revealing a highly elongated molecule with leucine-rich repeats that bind Met at one end, and GW domains that dissociably bind the bacterial surface at the other. Surprisingly, the GW domains are seen to resemble SH3 domains. Despite this, GW domains are unlikely to act as functional mimics of SH3 domains since their potential proline-binding sites are blocked or destroyed. However, we do show that the GW domains, in addition to binding glycosaminoglycans, bind gC1q-R specifically, and that this binding requires release of InlB from the bacterial surface. Dissociable attachment to the bacterial surface via the GW domains may be responsible for restricting Met activation to a small, localized area of the host cell and for coupling InlB-induced host membrane dynamics with bacterial proximity during invasion. |
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| Keywords: cell invasion, gC1q-R, GW domain, internalin, SH3 domain |
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