Dual function of a bacterial protein as an adhesin and extracellular effector of host GTPase signaling.

Stones, Daniel H ORCID: 0000-0002-8981-7943 and Krachler, Anne Marie (2015) Dual function of a bacterial protein as an adhesin and extracellular effector of host GTPase signaling. Small GTPases, 6 (3). pp. 153-156. doi:10.1080/21541248.2015.1028609

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Bacterial pathogens often target conserved cellular mechanisms within their hosts to rewire signaling pathways and facilitate infection. Rho GTPases are important nodes within eukaryotic signaling networks and thus constitute a common target of pathogen-mediated manipulation. A diverse array of microbial mechanisms exists to interfere with Rho GTPase signaling. While targeting of GTPases by secreted bacterial effectors is a well-known strategy bacterial pathogens employ to interfere with the host, we have recently described pathogen adhesion as a novel extracellular stimulus that hijacks host GTPase signaling. The Multivalent Adhesion Molecule MAM7 from Vibrio parahaemolyticus directly binds host cell membrane lipids. The ensuing coalescence of phosphatidic acid ligands in the host membrane leads to downstream activation of RhoA and actin rearrangements. Herein, we discuss mechanistic models of lipid-mediated Rho activation and the implications from the infected host’s and the pathogen’s perspective.

Item Type: Article
Article Type: Article
Uncontrolled Keywords: Actin dynamics; Adhesin; Effector; Host-pathogen interaction; Lipid signaling; Phosphatidic acid; Rho GTPases; RhoA; Vibrio
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QR Microbiology
Divisions: Schools and Research Institutes > School of Education and Science
Research Priority Areas: Place, Environment and Community
Depositing User: Rhiannon Goodland
Date Deposited: 04 Jul 2018 10:50
Last Modified: 31 Aug 2023 08:58
URI: https://eprints.glos.ac.uk/id/eprint/5756

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