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• W1541686136 endingPage "6227" @default.
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• W1541686136 abstract "ABSTRACT Most details of the processing of the hepatitis A virus (HAV) polyprotein are known. Unique among members of the family Picornaviridae , the primary cleavage of the HAV polyprotein is mediated by 3C pro , the only proteinase known to be encoded by the virus, at the 2A/2B junction. All other cleavages of the polyprotein have been considered to be due to 3C pro , although the precise location and mechanism responsible for the VP1/2A cleavage have been controversial. Here we present data that argue strongly against the involvement of the HAV 3C pro proteinase in the maturation of VP1 from its VP1-2A precursor. Using a heterologous expression system based on recombinant vaccinia viruses directing the expression of full-length or truncated capsid protein precursors, we show that the C terminus of the mature VP1 capsid protein is located near residue 764 of the polyprotein. However, a proteolytically active HAV 3C pro that was capable of directing both VP0/VP3 and VP3/VP1 cleavages in vaccinia virus-infected cells failed to process the VP1-2A precursor. Using site-directed mutagenesis of an infectious molecular clone of HAV, we modified potential VP1/2A cleavage sites that fit known 3C pro recognition criteria and found that a substitution that ablates the presumed 3C pro dipeptide recognition sequence at Glu 764 -Ser 765 abolished neither infectivity nor normal VP1 maturation. Altered electrophoretic mobility of VP1 from a viable mutant virus with an Arg 764 substitution indicated that this residue is present in VP1 and that the VP1/2A cleavage occurs downstream of this residue. These data indicate that maturation of the HAV VP1 capsid protein is not dependent on 3C pro processing and may thus be uniquely dependent on a cellular proteinase." @default.
• W1541686136 created "2016-06-24" @default.
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• W1541686136 date "1999-08-01" @default.
• W1541686136 modified "2023-10-06" @default.
• W1541686136 title "Maturation of the Hepatitis A Virus Capsid Protein VP1 Is Not Dependent on Processing by the 3C ^pro Proteinase" @default.
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• W1541686136 doi "https://doi.org/10.1128/jvi.73.8.6220-6227.1999" @default.
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