Sialic acid dependence in rotavirus host cell invasion.
We used NMR spectroscopy, molecular modeling and infectivity competition assays to investigate the key interactions between the spike protein (VP8(*)) from 'sialidase-insensitive' human Wa and 'sialidase-sensitive' porcine CRW-8 rotaviruses and the glycans of gangliosides G(M1) and G(D1a). Our data provide strong evidence that N-acetylneuraminic acid is a key determinant for binding of these rotaviruses. This is in contrast to the widely accepted paradigm that sialic acids are irrelevant in host cell recognition by sialidase-insensitive rotaviruses.
Haselhorst
Thomas
T
Institute for Glycomics, Gold Coast Campus, Griffith University, Parklands Drive, Southport, Queensland 4222, Australia.
Fleming
Fiona E
FE
Dyason
Jeffrey C
JC
Hartnell
Regan D
RD
Yu
Xing
X
Holloway
Gavan
G
Santegoets
Kim
K
Kiefel
Milton J
MJ
Blanchard
Helen
H
Coulson
Barbara S
BS
von Itzstein
Mark
M
D009682:Magnetic Resonance Spectroscopy; D019158:N-Acetylneuraminic Acid / Q000378:metabolism*; D012401:Rotavirus / Q000378:metabolism / Q000472:pathogenicity*
D019158:N-Acetylneuraminic Acid