Journal
BIOCHEMICAL JOURNAL
Volume 444, Issue -, Pages 429-435Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20112101
Keywords
glycan receptor; glycosylation; haemagglutinin; H1N1; influenza virus.
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Funding
- National Institutes of Health [GM R37 GM057073-13]
- Singapore MIT Alliance for Research and Technology (SMART)
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The glycoprotein HA (haemagglutinin) on the surface of influenza A virus plays a central role in recognition and binding to specific host cell-surface glycan receptors and in fusion of viral membrane to the host nuclear membrane during viral replication. Given the abundance of HA on the viral surface, this protein is also the primary target for host innate and adaptive immune responses. Although addition of glycosylation sites on HA are a part of viral evolution to evade the host immune responses, there are specific glycosylation sites that are conserved during most of the evolution of the virus. In the present study, it was demonstrated that one such conserved glycosylation site at Asn(91) in H1N1 HA critically governs the glycan receptor-binding specificity and hence would potentially impinge on the host adaptation of the virus.
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