Two glycosylation sites in H5N1 influenza virus hemagglutinin that affect binding preference by computer-based analysis.

Increasing numbers of H5N1 influenza viruses (IVs) are responsible for human deaths, especially in North Africa and Southeast Asian. The binding of hemagglutinin (HA) on the viral surface to host sialic acid (SA) receptors is a requisite step in the infection process. Phylogenetic analysis reveals t...

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Autores principales:	Wentian Chen, Shisheng Sun, Zheng Li
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/15cf487e0ba648b88da9b6b939dd4b0e
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spelling	oai:doaj.org-article:15cf487e0ba648b88da9b6b939dd4b0e2021-11-18T07:15:30ZTwo glycosylation sites in H5N1 influenza virus hemagglutinin that affect binding preference by computer-based analysis.1932-620310.1371/journal.pone.0038794https://doaj.org/article/15cf487e0ba648b88da9b6b939dd4b0e2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22719948/?tool=EBIhttps://doaj.org/toc/1932-6203Increasing numbers of H5N1 influenza viruses (IVs) are responsible for human deaths, especially in North Africa and Southeast Asian. The binding of hemagglutinin (HA) on the viral surface to host sialic acid (SA) receptors is a requisite step in the infection process. Phylogenetic analysis reveals that H5N1 viruses can be divided into 10 clades based on their HA sequences, with most human IVs centered from clade 1 and clade 2.1 to clade 2.3. Protein sequence alignment in various clades indicates the high conservation in the receptor-binding domains (RBDs) is essential for binding with the SA receptor. Two glycosylation sites, 158N and 169N, also participate in receptor recognition. In the present work, we attempted to construct a serial H5N1 HA models including diverse glycosylated HAs to simulate the binding process with various SA receptors in silico. As the SA-α-2,3-Gal and SA-α-2,6-Gal receptor adopted two distinctive topologies, straight and fishhook-like, respectively, the presence of N-glycans at 158N would decrease the affinity of HA for all of the receptors, particularly SA-α-2,6-Gal analogs. The steric clashes of the huge glycans shown at another glycosylation site, 169N, located on an adjacent HA monomer, would be more effective in preventing the binding of SA-α-2,3-Gal analogs.Wentian ChenShisheng SunZheng LiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 6, p e38794 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Wentian Chen Shisheng Sun Zheng Li Two glycosylation sites in H5N1 influenza virus hemagglutinin that affect binding preference by computer-based analysis.
description	Increasing numbers of H5N1 influenza viruses (IVs) are responsible for human deaths, especially in North Africa and Southeast Asian. The binding of hemagglutinin (HA) on the viral surface to host sialic acid (SA) receptors is a requisite step in the infection process. Phylogenetic analysis reveals that H5N1 viruses can be divided into 10 clades based on their HA sequences, with most human IVs centered from clade 1 and clade 2.1 to clade 2.3. Protein sequence alignment in various clades indicates the high conservation in the receptor-binding domains (RBDs) is essential for binding with the SA receptor. Two glycosylation sites, 158N and 169N, also participate in receptor recognition. In the present work, we attempted to construct a serial H5N1 HA models including diverse glycosylated HAs to simulate the binding process with various SA receptors in silico. As the SA-α-2,3-Gal and SA-α-2,6-Gal receptor adopted two distinctive topologies, straight and fishhook-like, respectively, the presence of N-glycans at 158N would decrease the affinity of HA for all of the receptors, particularly SA-α-2,6-Gal analogs. The steric clashes of the huge glycans shown at another glycosylation site, 169N, located on an adjacent HA monomer, would be more effective in preventing the binding of SA-α-2,3-Gal analogs.
format	article
author	Wentian Chen Shisheng Sun Zheng Li
author_facet	Wentian Chen Shisheng Sun Zheng Li
author_sort	Wentian Chen
title	Two glycosylation sites in H5N1 influenza virus hemagglutinin that affect binding preference by computer-based analysis.
title_short	Two glycosylation sites in H5N1 influenza virus hemagglutinin that affect binding preference by computer-based analysis.
title_full	Two glycosylation sites in H5N1 influenza virus hemagglutinin that affect binding preference by computer-based analysis.
title_fullStr	Two glycosylation sites in H5N1 influenza virus hemagglutinin that affect binding preference by computer-based analysis.
title_full_unstemmed	Two glycosylation sites in H5N1 influenza virus hemagglutinin that affect binding preference by computer-based analysis.
title_sort	two glycosylation sites in h5n1 influenza virus hemagglutinin that affect binding preference by computer-based analysis.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/15cf487e0ba648b88da9b6b939dd4b0e
work_keys_str_mv	AT wentianchen twoglycosylationsitesinh5n1influenzavirushemagglutininthataffectbindingpreferencebycomputerbasedanalysis AT shishengsun twoglycosylationsitesinh5n1influenzavirushemagglutininthataffectbindingpreferencebycomputerbasedanalysis AT zhengli twoglycosylationsitesinh5n1influenzavirushemagglutininthataffectbindingpreferencebycomputerbasedanalysis
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Two glycosylation sites in H5N1 influenza virus hemagglutinin that affect binding preference by computer-based analysis.

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