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). pp. 7221-7229.

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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 ofAfrican 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.

Item Type:	Article
Faculty \ School:	Faculty of Medicine and Health Sciences > Norwich Medical School
UEA Research Groups:	Faculty of Medicine and Health Sciences > Research Groups > Medicine (former - to 2013) Faculty of Medicine and Health Sciences > Research Groups > Gastroenterology and Gut Biology Faculty of Medicine and Health Sciences > Research Centres > Metabolic Health Faculty of Medicine and Health Sciences > Research Centres > Lifespan Health
Depositing User:	EPrints Services
Date Deposited:	25 Nov 2010 11:09
Last Modified:	12 Jun 2024 14:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/12372
DOI:	10.1128/JVI.75.16.7221-7229.2001

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