VP7 mediates the interaction of rotaviruses with integrin alphavbeta3 through a novel integrin-binding site.
Zárate
Selene
S
Departamento de Génetica del Desarrollo y Fisiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Col. Chamilpa, Cuernavaca, Morelos 62210, Mexico.
Romero
Pedro
P
Espinosa
Rafaela
R
Arias
Carlos F
CF
López
Susana
S
D000595:Amino Acid Sequence; D000818:Animals; D000956:Antigens, Viral / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D036022:Capsid Proteins / Q000737:chemistry* / Q000378:metabolism; D002460:Cell Line; D015967:Gene Expression Regulation, Viral; D039302:Integrin alphaVbeta3 / Q000378:metabolism*; D008253:Macaca mulatta / Q000821:virology; D008969:Molecular Sequence Data; D019158:N-Acetylneuraminic Acid / Q000378:metabolism; D012401:Rotavirus / Q000235:genetics / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
D000956:Antigens, Viral; D036022:Capsid Proteins; D039302:Integrin alphaVbeta3; C060339:VP4 protein, Rotavirus; C050779:VP7 protein, Rotavirus; D014357:Trypsin; D019158:N-Acetylneuraminic Acid