Preprint Hypothesis Version 1 Preserved in Portico This version is not peer-reviewed

Two Achilles' Heels of the Ebolavirus Glycoprotein?

Wei Li * ORCID logo
Version 1 : Received: 10 March 2020 / Approved: 11 March 2020 / Online: 11 March 2020 (10:32:02 CET)

How to cite: Li, W. Two Achilles' Heels of the Ebolavirus Glycoprotein?. Preprints 2020, 2020030183 (doi: 10.20944/preprints202003.0183.v1). Li, W. Two Achilles' Heels of the Ebolavirus Glycoprotein?. Preprints 2020, 2020030183 (doi: 10.20944/preprints202003.0183.v1).

Abstract

Ebolavirus has a membrane envelope decorated by trimers of a glycoprotein (GP), which is responsible for host cell attachment and membrane fusion. Therefore, GP is a primary target for antiviral drugs development. Here, this article reports the first, to my knowledge, set of structural analysis of all Ebolavirus GP structures as of March 10, 2020, and also a brief update of the structurally identified electrostatic features of the Ebolavirus GP structures in both apo (unliganded) state and also in bound states with a series of small compounds, including a variety of approved drugs. With this comprehensive set of structural analysis, this article puts forward a hypothesis of two Achilles' heels of Ebolavirus GP structure, where the formation of two interfacial salt bridges, instead of destabilizing the prefusion conformation of Ebolavirus GP, constitutes a positive contribution towards the structural rigidification of the prefusion conformation of the Ebolavirus GP structure, thereby acting against GP-mediated Ebolavirus cell entry and/or preventing fusion between the viral and endosome membranes.

Subject Areas

Ebolavirus glycoprotein; Electrostatic interaction; Salt bridging network; Two Achilles' heels

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