Journal of General Virology, Vol 79, 725-729, Copyright © 1998 by Society for General Microbiology

ARTICLES

Identification of mutations in the rotavirus protein VP4 that alter sialic-acid-dependent infection

JE Ludert, BB Mason, J Angel, B Tang, Y Hoshino, N Feng, PT Vo, EM Mackow, FM Ruggeri and HB Greenberg
Department of Medicine, Stanford University School of Medicine, CA 94305, USA. jeludert@pasteur.ivic.ve

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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