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      133 Structural basis for ebolavirus matrix assembly and budding; protein plasticity allows multiple functions

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          Abstract

          Proteins, particularly viral proteins, can be multifunctional, but the mechanism(s) behind this trait are not fully understood. Here, we illustrate through multiple crystal structures, biochemistry and cellular microscopy that the Ebola virus VP40 protein rearranges into different structures, each with a distinct and essential function required for the ebolavirus life cycle. A butterfly-shaped VP40 dimer trafficks to the cellular membrane. There, electrostatic interactions trigger rearrangement of the polypeptide into a linear hexamer. These hexamers construct a multi-layered, filamentous matrix structure that is critical for budding and resembles tomograms of authentic virions. A third structure of VP40, formed by a different rearrangement, is not involved in virus assembly, but instead uniquely binds RNA to regulate viral transcription inside infected cells. These results provide a functional model for ebolavirus matrix assembly and the other roles of VP40 in the virus life cycle, and demonstrate how a single, wild-type, unmodified polypeptide can assemble into different structures for different functions.

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          Author and article information

          Journal
          J Acquir Immune Defic Syndr
          J. Acquir. Immune Defic. Syndr
          qai
          Journal of Acquired Immune Deficiency Syndromes (1999)
          JAIDS Journal of Acquired Immune Deficiency Syndromes
          1525-4135
          1944-7884
          April 2014
          07 March 2014
          : 65
          : Suppl 2 , 15th Annual International Meeting of the Institute of Human Virology
          : 55
          Affiliations
          The Scripps Research Institute, California, US
          Article
          00037
          10.1097/01.qai.0000446713.32982.25
          4149652
          6a86e632-0fa3-41ac-b7c7-4ff90575eed3
          Copyright © 2014 by Lippincott Williams & Wilkins

          This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivitives 3.0 License, where it is permissible to download and share the work provided it is properly cited. The work cannot be changed in any way or used commercially.

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          Abstract
          Abstracts—September 10, 2013 (Day 3)

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