Journal of Virology, August 2001, p. 7221-7229, Vol. 75, No. 16
Department of Immunology, Institute for
Animal Health, Pirbright Laboratory, Woking, Surrey GU24 ONF,
United Kingdom
Received 22 December 2000/Accepted 15 May 2001
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.
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.16.7221-7229.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
A Virally Encoded Chaperone Specialized for Folding
of the Major Capsid Protein of African Swine Fever Virus
*
Corresponding author. Mailing address: Institute
for Animal Health, Pirbright Laboratory, Ash Road, Woking, Surrey
GU24 ONF, United Kingdom. Phone: 44-1483-232441. Fax:
44-1483-232448. E-mail: thomas.wileman{at}bbsrc.ac.uk.
Journal of Virology, August 2001, p. 7221-7229, Vol. 75, No. 16
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.16.7221-7229.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
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