Journal of Virology · 2012 · 253 citations · 50 references
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, Séverine Marionneau‐Lambot et al. · The Journal of Infectious Diseases · 2003 · 411 citations
Virus Structure, Viruslike Particles, Distinct Strain‐specific Patterns +15
Stefan Taube, Jeffrey W. Perry, Kristen D. Yetming et al. · Journal of Virology · 2009 · 199 citations · Full text
Primary Murine Macrophages, Molecular Virology, Murine Norovirus 1 +11