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

摘要: It is generally believed that cellular chaperones facilitate the folding of virus capsid proteins, or proteins fold spontaneously. Here we show p73, major protein African swine fever (ASFV) failed to and aggregated when expressed alone in cells. This demonstrated were unable aid p73 suggested ASFV may encode a chaperone. An 80-kDa encoded by ASFV, termed capsid-associated (CAP) 80, bound newly synthesized infected The was released following conformational maturation dissociated before assembly. Coexpression with prevented aggregation allowed kinetics identical those seen CAP80 is, therefore, virally chaperone facilitates masking domains exposed protein, which are susceptible aggregation, but cannot be accommodated host chaperones. likely these ultimately buried added growing shell.