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• W2134661630 endingPage "1563" @default.
• W2134661630 startingPage "1556" @default.
• W2134661630 abstract "The capsid (C) protein of alphaviruses consists of two protein domains: a serine protease at the COOH terminus and an NH2-terminal domain which is thought to interact with RNA in the virus nucleocapsid (NC). The latter domain is very rich in positively charged amino acid residues. In this work, we have introduced large deletions into the corresponding region of a full-length cDNA clone of Semliki Forest virus, expressed the transcribed RNA in BHK-21 cells, and monitored the autoprotease activity of C, the formation of intracellular NCs, and the release of infectious virus. Our results show that if the gene region encoding the whole NH2-terminal domain is removed, the expressed C protein fragment cannot assemble into NCs and virus particles but it is still able to function as an autoprotease. Thus, these results underline the general importance of the NH2-terminal domain in the virus assembly process and furthermore show that the serine protease domain can function independently of the NH2 terminus. Surprisingly, analysis of additional C protein deletion variants showed that not all of the NH2-terminal domain is required for virus assembly, but large deletions involving up to one-third of its positively charged residues are still compatible with NC and virus formation. The fact that so much flexibility is allowed in the structure of the NH2-terminal domain of C suggests that most of this region is involved in nonspecific interactions with the encapsidated RNA, probably through its positively charged amino acid residues." @default.
• W2134661630 created "2016-06-24" @default.
• W2134661630 creator A5001072062 @default.
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• W2134661630 date "1995-03-01" @default.
• W2134661630 modified "2023-10-01" @default.
• W2134661630 title "Structure-function relation of the NH2-terminal domain of the Semliki Forest virus capsid protein" @default.
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• W2134661630 doi "https://doi.org/10.1128/jvi.69.3.1556-1563.1995" @default.
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