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Composite Model of Full GP Structure of Ebola Virus Envelope Glycoprotein | OMICS International
ISSN: 1747-0862
Journal of Molecular and Genetic Medicine
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Composite Model of Full GP Structure of Ebola Virus Envelope Glycoprotein

Garry William Lynch*

University of Sydney, Australia

Corresponding Author:
Garry William Lynch
Senior Lecturer/Senior Research Fellow
University of Sydney
Faculties of Medicine & Veterinary Science
Rm 551 Gunn Bldg (B19)
Sydney, NSW 2006, Australia
E-mail: [email protected]

Received date March 27, 2015; Accepted date March 29, 2015; Published date April 06, 2015

Citation: Lynch GM (2015) Composite Model of Full GP Structure of Ebola Virus Envelope Glycoprotein. J Mol Genet Med 9:i101. doi:10.4172/1747-0862.1000I101

Copyright: © 2015 Lynch GM. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Description

Depicted is a composite model of the Ebola surface glycoprotein (GP) in its trimeric configuration (monomers comprise GP1GP2 subunits) and represents a single GP spike projecting from the surface of the Ebola Virus. This figure combines the published X-ray crystallographic (core) and cryoelectron tomography (global) structures, together now with in silico modeled sections of the mucin-like domain and separately the GP stalk. The latter are missing from earlier published crystal structure determinations. The core Ebola Virus glycoprotein GP 3CSY structure (of homo-trimers of truncated GP1-GP2 monomers) was determined by x-ray crystallography at 3.4 Angstroms and is shown both at the bottom left (space filled depiction) and in the centre of the image within a composite model (white – in protein cartoon structure depiction). In silico modeling with Phyre was performed to obtain a structural model of the GP mucin-like domain (space filled top right monomer), and also incorporated into the central composite image (yellow – top). An in silico model for the GP membrane proximal stalk domain was additionally composed and is represented in trimeric configuration (space filled - bottom right) and in the centre composite (yellow strands – at the bottom). These in silico modelled structures are mapped into the composite shown in the centre with 3 separate mucin-like domains represented in yellow at the top of the trimer model, and at the base of that structure a homotrimeric stem (also in yellow). Together these components: the mucin-like (in silico modeled), core binding and fusion (x-ray crystal defined) and GP-membrane stalk (in situ modeled) regions cover the whole GP (i.e. GP1+GP2) monomer sequence and represent the pre-fusion conformation. These have been mapped in 3D space as trimers, and dispayed within the GP structure framework provided by the cryo-electron tomograph of the global GP trimer configuration.

The tomograph is shown in surface view in the top left of the figure and in the central composite image as a blue mesh background. Note: the structures of the central composite are enlarged relative to their peripherally displayed individual elements.

molecular-genetic-trimeric-prefusion

Figure 1: Compilation of a full trimeric prefusion model of the Ebola virus (EBOV) surface envelope glycoprotein GP.

 

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