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Mapping the Structure and Function of the E1 and E2 Glycoproteins in Alphaviruses

Mukhopadhyay, Suchetana and Zhang, Wei and Gabler, Stefan and Chipman, Paul R. and Strauss, Ellen G. and Strauss, James H. and Baker, Timothy S. and Kuhn, Richard J. and Rossmann, Michael G. (2006) Mapping the Structure and Function of the E1 and E2 Glycoproteins in Alphaviruses. Structure, 14 (1). pp. 63-73. ISSN 09692126. PMCID PMC2757649. https://resolver.caltech.edu/CaltechAUTHORS:20160111-150851171

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Abstract

The 9 Å resolution cryo-electron microscopy map of Sindbis virus presented here provides structural information on the polypeptide topology of the E2 protein, on the interactions between the E1 and E2 glycoproteins in the formation of a heterodimer, on the difference in conformation of the two types of trimeric spikes, on the interaction between the transmembrane helices of the E1 and E2 proteins, and on the conformational changes that occur when fusing with a host cell. The positions of various markers on the E2 protein established the approximate topology of the E2 structure. The largest conformational differences between the icosahedral surface spikes at icosahedral 3-fold and quasi-3-fold positions are associated with the monomers closest to the 5-fold axes. The long E2 monomers, containing the cell receptor recognition motif at their extremities, are shown to rotate by about 180^o and to move away from the center of the spikes during fusion.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1016/j.str.2005.07.025 showDOIArticle
http://www.cell.com/structure/references/S0969-2126%2805%2900393-XPublisherArticle
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2757649/PubMed CentralArticle
Additional Information:© Elsevier Ltd. Received: May 10, 2005. Revised: July 11, 2005. Accepted: July 16, 2005. Published: January 10, 2006. We thank Rob Ashmore and Chuan Xiao for developing and maintaining numerous computer and interactive graphic programs, and Ying Zhang and Petr Leiman for helpful discussions and Jolanda Smit for purified SFV. The work was supported in part by National Institutes of Health (NIH) Program Project Grant (AI55672) to T.S.B., R.J.K., M.G.R., and J.H.S., and by NIH grants to T.S.B. (GM R37-033050), R.J.K. (GM56279), and J.H.S. (AI20612). Accession Numbers: The 9Å cryo-EM map has been deposited with the European Bioinformatics Institute under accession code EMD-1121. The coordinates of the fitted ectodomain E1, transmembranes E1 and E2, and the capsid protein have been deposited with the Protein Data Bank under accession code 1Z8Y.
Funders:
Funding AgencyGrant Number
NIHAI55672
NIHGM R37-033050
NIHGM56279
NIHAI20612
Issue or Number:1
PubMed Central ID:PMC2757649
Record Number:CaltechAUTHORS:20160111-150851171
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20160111-150851171
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:63550
Collection:CaltechAUTHORS
Deposited By: Donna Wrublewski
Deposited On:12 Jan 2016 23:27
Last Modified:03 Oct 2019 09:29

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