@article{mbs:/content/journal/jgv/10.1099/0022-1317-79-4-725, author = "Ludert, Juan E and Mason, Bruce B and Angel, Juana and Tang, Baozhang and Hoshino, Yasutaka and Feng, Ningguo and Vo, Phuoc T and Mackow, Erick M and Ruggeri, Franco M and Greenberg, Harry B", title = "Identification of mutations in the rotavirus protein VP4 that alter sialic-acid-dependent infection.", journal= "Journal of General Virology", year = "1998", volume = "79", number = "4", pages = "725-729", doi = "https://doi.org/10.1099/0022-1317-79-4-725", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-79-4-725", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", 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 × 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.", }