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  • Title: Identification of mutations in the rotavirus protein VP4 that alter sialic-acid-dependent infection.
    Author: Ludert JE, Mason BB, Angel J, Tang B, Hoshino Y, Feng N, Vo PT, Mackow EM, Ruggeri FM, Greenberg HB.
    Journal: J Gen Virol; 1998 Apr; 79 ( Pt 4)():725-9. PubMed ID: 9568967.
    Abstract:
    To explore further the role of VP4 as the rotavirus cell attachment protein, VP7 monoreassortants derived from the sialic-acid-dependent simian strain RRV and from the sialic-acid-independent human strains D, DS-1 and ST-3 were tested for susceptibility of infectivity of neuraminidase-treated MA-104 cells. Infectivity of RRV x D VP7 and RRV x ST-3 VP7 monoreassortants decreased when sialic acid was removed from the cell surface. However, of three separate RRV x DS-1 VP7 monoreassortants tested, only one was sialic-acid-dependent. Sequence analysis showed that both sialic-acid-independent strains contained a single amino acid change, Lys to Arg, at position 187. In addition, sialic-acid-independent infectivity was seen in one of 14 RRV VP4 neutralization escape mutants tested, and this strain was found to have a Gly to Glu change at amino acid position 150. These results indicate that positions 150 and 187 of VP4 play an important role in early rotavirus-cell interactions.
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