Identification of mutations in the rotavirus protein VP4 that alter sialic-acid-dependent infection.
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.
Ludert
J E
JE
Department of Medicine, Stanford University School of Medicine, CA 94305, USA. jeludert@pasteur.ivic.ve
Mason
B B
BB
Angel
J
J
Tang
B
B
Hoshino
Y
Y
Feng
N
N
Vo
P T
PT
Mackow
E M
EM
Ruggeri
F M
FM
Greenberg
H B
HB
D000818:Animals; D000956:Antigens, Viral; D002213:Capsid / Q000235:genetics* / Q000378:metabolism; D036022:Capsid Proteins; D002460:Cell Line; D005814:Genes, Viral; D006801:Humans; D008253:Macaca mulatta; D019158:N-Acetylneuraminic Acid / Q000378:metabolism*; D009439:Neuraminidase; D017354:Point Mutation; D012401:Rotavirus / Q000235:genetics* / Q000378:metabolism / Q000472:pathogenicity*; D014774:Virulence / Q000235:genetics
D000956:Antigens, Viral; D036022:Capsid Proteins; C060339:VP4 protein, Rotavirus; C050779:VP7 protein, Rotavirus; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid