A virally encoded chaperone specialised for folding of the major capsid protein of African swine fever virus

Cobbold, C., Windsor, M. and Wileman, T. (2001) A virally encoded chaperone specialised for folding of the major capsid protein of African swine fever virus. Journal of Virology, 75 16: 7221-7229.


Author Cobbold, C.
Windsor, M.
Wileman, T.
Title A virally encoded chaperone specialised for folding of the major capsid protein of African swine fever virus
Journal name Journal of Virology   Check publisher's open access policy
ISSN 0022-538X
Publication date 2001-08
Sub-type Article (original research)
DOI 10.1128/JVI.75.16.7221-7229.2001
Volume 75
Issue 16
Start page 7221
End page 7229
Total pages 9
Place of publication Washington, D.C., USA
Publisher American Society for Microbiology
Language eng
Subject 1103 Clinical Sciences
0605 Microbiology
Formatted abstract It is generally believed that cellular chaperones facilitate the folding of virus capsid proteins, or that capsid proteins fold spontaneously. Here we show that p73, the major capsid protein of African swine fever virus (ASFV) failed to fold and aggregated when expressed alone in cells. This demonstrated that cellular chaperones were unable to aid the folding of p73 and suggested that ASFV may encode a chaperone. An 80-kDa protein encoded by ASFV, termed the capsid-associated protein (CAP) 80, bound to the newly synthesized capsid protein in infected cells. The 80-kDa protein was released following conformational maturation of p73 and dissociated before capsid assembly. Coexpression of the 80-kDa protein with p73 prevented aggregation and allowed the capsid protein to fold with kinetics identical to those seen in infected cells. CAP80 is, therefore, a virally encoded chaperone that facilitates capsid protein folding by masking domains exposed by the newly synthesized capsid protein, which are susceptible to aggregation, but cannot be accommodated by host chaperones. It is likely that these domains are ultimately buried when newly synthesized capsid proteins are added to the growing capsid shell.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Biomedical Sciences Publications
 
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