Document Detail


The alphavirus E3 glycoprotein functions in a clade-specific manner.
MedLine Citation:
PMID:  23035234     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The 80 trimeric, glycoprotein spikes that cover the surface of alphavirus particles are required for mediating viral entry into a host cell. Spike assembly is a regulated process that requires interactions between five structural proteins, E3, E2, 6K and its translational frameshift product TF, and E1. E3 is a small, ∼65-amino-acid glycoprotein that has two known functions: E3 serves as the signal sequence for translocation of the E3-E2-6K-E1 polyprotein into the endoplasmic reticulum (ER), and cleavage of E3 from E2 is essential for virus maturation. Nonetheless, when E3 is replaced with an ER signal sequence, spikes do not form and infectious particles are not assembled, suggesting an additional role(s) for E3 in the viral life cycle. To further investigate the role of E3 in spike assembly, we made chimeric viruses in which E3 from one alphavirus species is replaced with E3 from another species. Our results demonstrate that when E3 is interchanged between alphavirus species that belong to the same virus clade, viral titers and particle morphologies and compositions are similar to what are observed for the parental virus. In contrast, for chimeras in which E3 is derived from a different clade than the parental virus, we observed reduced titers and the formation of particles with atypical morphologies and protein compositions. We further characterized the E3 chimeras using a combination of structure-function and revertant analyses. This work revealed two specific interactions between E3 and its cognate E2 glycoprotein that are important for regulating spike assembly.
Authors:
Anthony J Snyder; Suchetana Mukhopadhyay
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-10-03
Journal Detail:
Title:  Journal of virology     Volume:  86     ISSN:  1098-5514     ISO Abbreviation:  J. Virol.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-11-20     Completed Date:  2013-01-28     Revised Date:  2013-07-11    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  13609-20     Citation Subset:  IM    
Affiliation:
Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana, USA.
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MeSH Terms
Descriptor/Qualifier:
Alphavirus / metabolism,  physiology*
Amino Acid Sequence
Animals
Base Sequence
Cell Line
Cricetinae
DNA Primers
Glycoproteins / chemistry,  physiology*
Microscopy, Electron, Transmission
Molecular Sequence Data
Reverse Transcriptase Polymerase Chain Reaction
Sequence Homology, Amino Acid
Viral Proteins / chemistry,  physiology*
Grant Support
ID/Acronym/Agency:
T32-GM007757/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/DNA Primers; 0/Glycoproteins; 0/Viral Proteins
Comments/Corrections

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