%0 Journal Article %A Ludert, Juan E %A Mason, Bruce B %A Angel, Juana %A Tang, Baozhang %A Hoshino, Yasutaka %A Feng, Ningguo %A Vo, Phuoc T %A Mackow, Erick M %A Ruggeri, Franco M %A Greenberg, Harry B %T Identification of mutations in the rotavirus protein VP4 that alter sialic-acid-dependent infection. %D 1998 %J Journal of General Virology, %V 79 %N 4 %P 725-729 %@ 1465-2099 %R https://doi.org/10.1099/0022-1317-79-4-725 %I Microbiology Society, %X 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 × D VP7 and RRV × ST-3 VP7 monoreassortants decreased when sialic acid was removed from the cell surface. However, of three separate RRV × 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. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-79-4-725