A glycerophospholipid-specific pocket in the RVFV class II fusion protein drives target membrane insertion

Science
P Guardado-CalvoF A Rey

Abstract

The Rift Valley fever virus (RVFV) is transmitted by infected mosquitoes, causing severe disease in humans and livestock across Africa. We determined the x-ray structure of the RVFV class II fusion protein Gc in its postfusion form and in complex with a glycerophospholipid (GPL) bound in a conserved cavity next to the fusion loop. Site-directed mutagenesis and molecular dynamics simulations further revealed a built-in motif allowing en bloc insertion of the fusion loop into membranes, making few nonpolar side-chain interactions with the aliphatic moiety and multiple polar interactions with lipid head groups upon membrane restructuring. The GPL head-group recognition pocket is conserved in the fusion proteins of other arthropod-borne viruses, such as Zika and chikungunya viruses, which have recently caused major epidemics worldwide.

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Citations

Dec 27, 2018·Cellular Microbiology·Alberto Fernández-OlivaCristina Risco
Nov 30, 2019·Journal of Biomolecular Structure & Dynamics·Laureano E Carpio, José Villalaín
Apr 22, 2020·ELife·Paul J Wichgers SchreurJeroen Kortekaas
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Aug 22, 2021·Proceedings of the National Academy of Sciences of the United States of America·Baldeep KhareRichard J Kuhn
Feb 14, 2019·Chemical Reviews·Valentina CorradiD Peter Tieleman
Aug 22, 2021·Current Opinion in Virology·Pablo Guardado-Calvo, Félix A Rey
Aug 29, 2021·Pathogens·Margarita V Rangel, Kenneth A Stapleford

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