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• W2208366175 abstract "The RNA replicase proteins of Semliki Forest virus (SFV) are translated as a P1234 polyprotein precursor that contains two putative autoproteases. Point mutations introduced into the predicted active sites of both proteases nsP2 (P2) and nsP4 (P4), separately or in combination, completely abolished virus replication in mammalian cells. The effects of these mutations on polyprotein processing were studied by in vitro translation and by expression of wild-type polyproteins P1234, P123, P23, P34 and their mutated counterparts in insect cells using recombinant baculoviruses. A mutation in the catalytic site of the P2 protease, C 478 A, (P2 CA ) completely abolished the processing of P12 CA 34, P12 CA 3 and P2 CA 3. Co-expression of P23 and P12 CA 34 in insect cells resulted in in trans cleavages at the P2/3 and P3/4 sites. Co-expression of P23 and P34 resulted in cleavage at the P3/4 site. In contrast, a construct with a mutation in the active site of the putative P4 protease, D 6 A, (P1234 DA ) was processed like the wild-type protein. P34 or its truncated forms were not processed when expressed alone. In insect cells, P4 was rapidly destroyed unless an inhibitor of proteosomal degradation was used. It is concluded that P2 is the only protease needed for the processing of SFV polyprotein P1234. Analysis of the cleavage products revealed that P23 or P2 could not cleave the P1/2 site in trans ." @default.
• W2208366175 created "2016-06-24" @default.
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• W2208366175 date "2001-04-01" @default.
• W2208366175 modified "2023-10-18" @default.
• W2208366175 title "Proteolytic processing of Semliki Forest virus-specific non-structural polyprotein by nsP2 protease" @default.
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• W2208366175 doi "https://doi.org/10.1099/0022-1317-82-4-765" @default.
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