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Novel structural insights into rotavirus recognition of ganglioside glycan receptors

Journal Article


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 GM3 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. © 2011 Elsevier Ltd. All rights reserved.

UOW Authors


  •   Blanchard, Helen (external author)

Publication Date


  • 2011

Citation


  • Yu, X., Coulson, B. S., Fleming, F. E., Dyason, J. C., Von Itzstein, M., & Blanchard, H. (2011). Novel structural insights into rotavirus recognition of ganglioside glycan receptors. Journal of Molecular Biology, 413(5), 929-939. doi:10.1016/j.jmb.2011.09.005

Scopus Eid


  • 2-s2.0-80855132554

Start Page


  • 929

End Page


  • 939

Volume


  • 413

Issue


  • 5

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 GM3 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. © 2011 Elsevier Ltd. All rights reserved.

UOW Authors


  •   Blanchard, Helen (external author)

Publication Date


  • 2011

Citation


  • Yu, X., Coulson, B. S., Fleming, F. E., Dyason, J. C., Von Itzstein, M., & Blanchard, H. (2011). Novel structural insights into rotavirus recognition of ganglioside glycan receptors. Journal of Molecular Biology, 413(5), 929-939. doi:10.1016/j.jmb.2011.09.005

Scopus Eid


  • 2-s2.0-80855132554

Start Page


  • 929

End Page


  • 939

Volume


  • 413

Issue


  • 5