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Viruses 2016, 8(4), 112; doi:10.3390/v8040112

Measles Virus Fusion Protein: Structure, Function and Inhibition

1
Division of Experimental and Clinical Research, , Vetsuisse Faculty, University of Bern, Bremgartenstrasse 109a, Bern 3001, Switzerland
2
Clinical Neurology, Department of Veterinary Medicine, University of Cambridge, CB3 0ES, Cambridge, UK
3
Graduate School for Cellular and Biomedical Sciences, University of Bern, Bern 3012, Switzerland
4
Paul G. Allen School for Global Animal Health, Washington State University, Pullman, WA 99164, USA
5
Department of Veterinary Microbiology and Pathology, Washington State University, Pullman, WA 99164, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Richard K. Plemper
Received: 30 January 2016 / Revised: 26 March 2016 / Accepted: 14 April 2016 / Published: 21 April 2016
(This article belongs to the Special Issue Recent Progress in Measles Virus Research)
View Full-Text   |   Download PDF [1358 KB, uploaded 21 April 2016]   |  

Abstract

Measles virus (MeV), a highly contagious member of the Paramyxoviridae family, causes measles in humans. The Paramyxoviridae family of negative single-stranded enveloped viruses includes several important human and animal pathogens, with MeV causing approximately 120,000 deaths annually. MeV and canine distemper virus (CDV)-mediated diseases can be prevented by vaccination. However, sub-optimal vaccine delivery continues to foster MeV outbreaks. Post-exposure prophylaxis with antivirals has been proposed as a novel strategy to complement vaccination programs by filling herd immunity gaps. Recent research has shown that membrane fusion induced by the morbillivirus glycoproteins is the first critical step for viral entry and infection, and determines cell pathology and disease outcome. Our molecular understanding of morbillivirus-associated membrane fusion has greatly progressed towards the feasibility to control this process by treating the fusion glycoprotein with inhibitory molecules. Current approaches to develop anti-membrane fusion drugs and our knowledge on drug resistance mechanisms strongly suggest that combined therapies will be a prerequisite. Thus, discovery of additional anti-fusion and/or anti-attachment protein small-molecule compounds may eventually translate into realistic therapeutic options. View Full-Text
Keywords: measles virus; cell entry; fusion protein; structural changes; inhibitors and mechanisms of adaptation; neuroinvasion; membrane fusion measles virus; cell entry; fusion protein; structural changes; inhibitors and mechanisms of adaptation; neuroinvasion; membrane fusion
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).

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MDPI and ACS Style

Plattet, P.; Alves, L.; Herren, M.; Aguilar, H.C. Measles Virus Fusion Protein: Structure, Function and Inhibition. Viruses 2016, 8, 112.

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