Journal
JOURNAL OF VIROLOGY
Volume 76, Issue 20, Pages 10512-10517Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.76.20.10512-10517.2002
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Funding
- NCI NIH HHS [R37 CA013202, CA 13202, R01 CA013202] Funding Source: Medline
- NCRR NIH HHS [P41 RR 00995] Funding Source: Medline
- NIAID NIH HHS [K08 AI 001496] Funding Source: Medline
- NIGMS NIH HHS [GM 47467, P01 GM047467] Funding Source: Medline
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Nuclear magnetic resonance spectroscopy demonstrates that the rhesus rotavirus hemagglutinin specifically binds alpha-anomeric N-acetylneuraminic acid with a K-d of 1.2 mM. The hemagglutinin requires no additional carbohydrate moieties for binding, does not distinguish 3' from 6' sialyllactose, and has approximately tenfold lower affinity for N-glycolylneuraminic than for N-acetyineuraminic acid. The broad specificity and low affinity of sialic acid binding by the rotavirus hemagglutinin are consistent with this interaction mediating initial cell attachment prior to the interactions that determine host range and cell type specificity.
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