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Recognition of the GM3 ganglioside glycan by rhesus rotavirus particles

Journal Article


Abstract


  • The tie that binds: Rotaviruses bind to their host cells through the interaction of the virion outer capsid and spike proteins with receptors including sialic acid containing glycoconjugates. Intact rotavirus particles interact with the glycan of the GM3 ganglioside (see picture) primarily through the N-acetylneuraminic acid, but the penultimate galactose residue also contributes. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Publication Date


  • 2011

Citation


  • Haselhorst, T., Fiebig, T., Dyason, J. C., Fleming, F. E., Blanchard, H., Coulson, B. S., & Von Itzstein, M. (2011). Recognition of the GM3 ganglioside glycan by rhesus rotavirus particles. Angewandte Chemie - International Edition, 50(5), 1055-1058. doi:10.1002/anie.201004116

Scopus Eid


  • 2-s2.0-79251589902

Start Page


  • 1055

End Page


  • 1058

Volume


  • 50

Issue


  • 5

Abstract


  • The tie that binds: Rotaviruses bind to their host cells through the interaction of the virion outer capsid and spike proteins with receptors including sialic acid containing glycoconjugates. Intact rotavirus particles interact with the glycan of the GM3 ganglioside (see picture) primarily through the N-acetylneuraminic acid, but the penultimate galactose residue also contributes. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Publication Date


  • 2011

Citation


  • Haselhorst, T., Fiebig, T., Dyason, J. C., Fleming, F. E., Blanchard, H., Coulson, B. S., & Von Itzstein, M. (2011). Recognition of the GM3 ganglioside glycan by rhesus rotavirus particles. Angewandte Chemie - International Edition, 50(5), 1055-1058. doi:10.1002/anie.201004116

Scopus Eid


  • 2-s2.0-79251589902

Start Page


  • 1055

End Page


  • 1058

Volume


  • 50

Issue


  • 5