Download MendeleyNovel structural insights into rotavirus recognition of ganglioside glycan receptors.
Yu, X., Coulson, B.S., Fleming, F.E., Dyason, J.C., von Itzstein, M., Blanchard, H.(2011) J Mol Biol 413: 929-939
- PubMed: 21945555
- DOI: https://doi.org/10.1016/j.jmb.2011.09.005
- Primary Citation of Related Structures:
3SIS, 3SIT - PubMed Abstract:
Rotaviruses ubiquitously infect children under the age of 5, being responsible for more than half a million diarrhoeal deaths each year worldwide. Host cell oligosaccharides containing sialic acid(s) are critical for attachment by rotaviruses. However, to date, no detailed three-dimensional atomic model showing the exact rotavirus interactions with these glycoconjugate receptors has been reported. Here, we present the first crystallographic structures of the rotavirus carbohydrate-recognizing protein VP8* in complex with ganglioside G(M3) glycans. In combination with assessment of the inhibition of rotavirus infectivity by N-acetyl and N-glycolyl forms of this ganglioside, our results reveal key details of rotavirus-ganglioside G(M3) glycan recognition. In addition, they show a direct correlation between the carbohydrate specificities exhibited by VP8* from porcine and by monkey rotaviruses and the respective infectious virus particles. These novel results also indicate the potential binding interactions of rotavirus VP8* with other sialic acid-containing gangliosides.
Organizational Affiliation:
Institute for Glycomics, Gold Coast campus, Griffith University, Queensland 4222, Australia.
