His-154 in the Gag protein of the L-A double-stranded RNA virus is essential for covalent linkage to the mRNA cap structure and for M1 satellite virus expression.
May guide antiviral targeting of viral cap linkage; extends mechanistic insights in animal models but leaves open therapeutic translation.
The coat protein (Gag) of the double-stranded RNA virus L-A was previously shown to form a covalent bond with the cap structure of eukaryotic mRNAs. Here, we identify the linkage as a phosphoroimidazole bond between the alpha phosphate of the cap structure and a nitrogen in the Gag protein His-154 imidazole side chain. Mutations of His-154 abrogate the ability of Gag to bind to the cap structure, without affecting cap recognition, in vivo virus particle formation from an L-A cDNA clone, or in vitro specific binding and replication of plus-stranded single-stranded RNA. However, genetic analyses demonstrate that His-154 is essential for M1 satellite virus expression.
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Blanc et al. (1994) studied this question.
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