Document Detail

Cryphonectria nitschkei virus 1 structure shows that the capsid protein of chrysoviruses is a duplicated helix-rich fold conserved in fungal double-stranded RNA viruses.
MedLine Citation:
PMID:  22593169     Owner:  NLM     Status:  MEDLINE    
Cryoelectron microscopy reconstruction of Cryphonectria nitschkei virus 1, a double-stranded RNA (dsRNA) virus, shows that the capsid protein (60 copies/particle) is formed by a repeated helical core, indicative of gene duplication. This unusual organization is common to chrysoviruses. The arrangement of many of these putative α-helices is conserved in the totivirus L-A capsid protein, suggesting a shared motif. Our results indicate that a 120-subunit T=1 capsid is a conserved architecture that optimizes dsRNA replication and organization.
Josué Gómez-Blanco; Daniel Luque; José M González; José L Carrascosa; Carlos Alfonso; Benes Trus; Wendy M Havens; Said A Ghabrial; José R Castón
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-05-16
Journal Detail:
Title:  Journal of virology     Volume:  86     ISSN:  1098-5514     ISO Abbreviation:  J. Virol.     Publication Date:  2012 Aug 
Date Detail:
Created Date:  2012-07-12     Completed Date:  2012-11-21     Revised Date:  2013-06-24    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  8314-8     Citation Subset:  IM    
Department of Structure of Macromolecules, Centro Nacional de Biotecnología/CSIC, Campus Cantoblanco, Madrid, Spain.
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MeSH Terms
Capsid Proteins / chemistry*,  metabolism
Protein Folding*
Protein Structure, Secondary
RNA Viruses / chemistry*,  physiology
RNA, Double-Stranded / biosynthesis
RNA, Viral / biosynthesis
Sordariales / virology*
Virus Replication / physiology
Reg. No./Substance:
0/Capsid Proteins; 0/RNA, Double-Stranded; 0/RNA, Viral

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