Plasma membrane association facilitates conformational changes in the Marburg virus protein VP40 dimer-Reference-Cited by-同舟云学术

Plasma membrane association facilitates conformational changes in the Marburg virus protein VP40 dimer

Published:2017 Issue:37 Volume:7 Page:22741-22748
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Bhattarai Nisha¹²³⁴^ORCID,GC Jeevan B.¹²³⁴^ORCID,Gerstman Bernard S.¹²³⁴⁵^ORCID,Stahelin Robert V.⁶⁷⁸⁹¹⁰,Chapagain Prem P.¹²³⁴⁵^ORCID

Affiliation:

1. Department of Physics

2. Florida International University

3. Miami

4. USA

5. Biomolecular Sciences Institute

6. Department of Chemistry and Biochemistry

7. The Eck Institute for Global Health

8. The Boler-Parseghian Center for Rare and Neglected Diseases

9. University of Notre Dame

10. Notre Dame

Abstract

The membrane binding interface of the Marburg virus protein mVP40 dimer differs from that of the Ebola virus eVP40 dimer but membrane binding allows conformational changes in mVP40 that makes it structurally similar to the eVP40 dimer.

Funder

National Institutes of Health

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2017/RA/C7RA02940C

Reference47 articles.

1. Proposal for a revised taxonomy of the family Filoviridae: classification, names of taxa and viruses, and virus abbreviations

2. Ebola and Marburg haemorrhagic fever

3. Virus Maturation by Budding

4. Ebola Virus VP40-Induced Particle Formation and Association with the Lipid Bilayer

5. Structural Rearrangement of Ebola Virus VP40 Begets Multiple Functions in the Virus Life Cycle

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