Journal of Virology · 2012 · 255 citations · 50 references
Life SciencesImmunologyInfectious DiseasesMolecular ImmunologyMolecular VirologyMucosal ImmunologyAntibody-antigen RecognitionAntigen RecognitionGastrointestinal ImmunologyPattern Recognition ReceptorsAntigen Specificity DeterminationImmune Recognition ReceptorsSialic Acid Recognition
Rotaviruses (RVs), an important cause of severe diarrhea in children, have been found to recognize sialic acid as receptors for host cell attachment. While a few animal RVs (of P[1], P[2], P[3], and P[7]) are sialidase sensitive, human RVs and the majority of animal RVs are sialidase insensitive. In this study, we demonstrated that the surface spike protein VP8* of the major P genotypes of human RVs interacts with the secretor histo-blood group antigens (HBGAs). Strains of the P[4] and P[8] genotypes shared reactivity with the common antigens of Lewis b (Le(b)) and H type 1, while strains of the P[6] genotype bound the H type 1 antigen only. The bindings between recombinant VP8* and human saliva, milk, or synthetic HBGA oligosaccharides were demonstrated, which was confirmed by blockade of the bindings by monoclonal antibodies (MAbs) specific to Le(b) and/or H type 1. In addition, specific binding activities were observed when triple-layered particles of a P[8] (Wa) RV were tested. Our results suggest that the spike protein VP8* of RVs is involved in the recognition of human HBGAs that may function as ligands or receptors for RV attachment to host cells.
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Pengwei Huang, Tibor Farkas, Weiming Zhong et al. · Journal of Virology · 2005 · 414 citations
Pengwei Huang, Tibor Farkas, Séverine Marionneau‐Lambot et al. · The Journal of Infectious Diseases · 2003 · 414 citations