Glycosylation at Asn[supscript 91] of H1N1 haemagglutinin affects binding to glycan receptors
Name
Sasisekharan_Glycosylation Asn91.pdf
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Author(s)
Jayaraman, Akila
Koh, Xiaoying
Li, Jing
Raman, Rahul
Viswanathan, Karthik
Shriver, Zachary H.
Sasisekharan, Ram
Date Issued
May 2012
Journal
Biochemical Journal
Publisher
Portland Press
Citation
Jayaraman, Akila et al. “Glycosylation at Asn [superscript 91] of H1N1 Haemagglutinin Affects Binding to Glycan Receptors.” Biochemical Journal 444.3 (2012).
Version
Final published version
Abstract
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[superscript 91] in H1N1 HA critically governs the glycan receptor-binding specificity and hence would potentially impinge on the host adaptation of the virus.
MIT Department
Harvard University--MIT Division of Health Sciences and Technology
Massachusetts Institute of Technology. Department of Biological Engineering
Massachusetts Institute of Technology. School of Engineering
Koch Institute for Integrative Cancer Research at MIT
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Creative Commons Attribution Non-Commercial License
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DOI of Published Version
https://doi.org/10.1042/BJ20112101
