tetano
Editor, Senior Moderator
Biochem J. 2012 Jun 15;444(3):429-35.
Glycosylation at Asn91 of H1N1 haemagglutinin affects binding to glycan receptors.
Jayaraman A, Koh X, Li J, Raman R, Viswanathan K, Shriver Z, Sasisekharan R.
Source
Harvard-MIT Division of Health Sciences and Technology, Koch Institute for Integrative Cancer Research, Singapore-MIT Alliance for Research and Technology, Department of Biological Engineering, Massachusetts Institute of Technology (MIT), 77 Massachusetts Avenue, Cambridge, MA 02139, U.S.A.
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 Asn91 in H1N1 HA critically governs the glycan receptor-binding specificity and hence would potentially impinge on the host adaptation of the virus.
PMID:
22642577
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/22642577
Glycosylation at Asn91 of H1N1 haemagglutinin affects binding to glycan receptors.
Jayaraman A, Koh X, Li J, Raman R, Viswanathan K, Shriver Z, Sasisekharan R.
Source
Harvard-MIT Division of Health Sciences and Technology, Koch Institute for Integrative Cancer Research, Singapore-MIT Alliance for Research and Technology, Department of Biological Engineering, Massachusetts Institute of Technology (MIT), 77 Massachusetts Avenue, Cambridge, MA 02139, U.S.A.
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 Asn91 in H1N1 HA critically governs the glycan receptor-binding specificity and hence would potentially impinge on the host adaptation of the virus.
PMID:
22642577
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/22642577