Next Article in Journal
Rhinoviruses and Respiratory Enteroviruses: Not as Simple as ABC
Next Article in Special Issue
Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M
Previous Article in Journal
The Influenza Virus H5N1 Infection Can Induce ROS Production for Viral Replication and Host Cell Death in A549 Cells Modulated by Human Cu/Zn Superoxide Dismutase (SOD1) Overexpression
Previous Article in Special Issue
Herpesvirus gB: A Finely Tuned Fusion Machine
Article Menu

Export Article

Open AccessReview
Viruses 2016, 8(1), 15; doi:10.3390/v8010015

Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane Fusion

Department of Medicinal Chemistry, University of Washington, Seattle, WA 98195, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Andrew Ward
Received: 20 October 2015 / Revised: 11 December 2015 / Accepted: 31 December 2015 / Published: 11 January 2016
(This article belongs to the Special Issue Viral Glycoprotein Structure)
View Full-Text   |   Download PDF [1693 KB, uploaded 11 January 2016]   |  

Abstract

The fusion glycoproteins that decorate the surface of enveloped viruses undergo dramatic conformational changes in the course of engaging with target cells through receptor interactions and during cell entry. These refolding events ultimately drive the fusion of viral and cellular membranes leading to delivery of the genetic cargo. While well-established methods for structure determination such as X-ray crystallography have provided detailed structures of fusion proteins in the pre- and post-fusion fusion states, to understand mechanistically how these fusion glycoproteins perform their structural calisthenics and drive membrane fusion requires new analytical approaches that enable dynamic intermediate states to be probed. Methods including structural mass spectrometry, small-angle X-ray scattering, and electron microscopy have begun to provide new insight into pathways of conformational change and fusion protein function. In combination, the approaches provide a significantly richer portrait of viral fusion glycoprotein structural variation and fusion activation as well as inhibition by neutralizing agents. Here recent studies that highlight the utility of these complementary approaches will be reviewed with a focus on the well-characterized influenza virus hemagglutinin fusion glycoprotein system. View Full-Text
Keywords: viral membrane fusion glycoprotein; structural mass spectrometry; electron microscopy; small-angle X-ray scattering; hydrogen-deuterium viral membrane fusion glycoprotein; structural mass spectrometry; electron microscopy; small-angle X-ray scattering; hydrogen-deuterium
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Garcia, N.K.; Lee, K.K. Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane Fusion. Viruses 2016, 8, 15.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Viruses EISSN 1999-4915 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top