Quantitative description of glycan-receptor binding of influenza A virus H7 hemagglutinin.

In the context of recently emerged novel influenza strains through reassortment, avian influenza subtypes such as H5N1, H7N7, H7N2, H7N3 and H9N2 pose a constant threat in terms of their adaptation to the human host. Among these subtypes, it was recently demonstrated that mutations in H5 and H9 hema...

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Autores principales:	Karunya Srinivasan, Rahul Raman, Akila Jayaraman, Karthik Viswanathan, Ram Sasisekharan
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/499a621c49524985979546b90469b036
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spelling	oai:doaj.org-article:499a621c49524985979546b90469b0362021-11-18T07:57:01ZQuantitative description of glycan-receptor binding of influenza A virus H7 hemagglutinin.1932-620310.1371/journal.pone.0049597https://doaj.org/article/499a621c49524985979546b90469b0362013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23437033/?tool=EBIhttps://doaj.org/toc/1932-6203In the context of recently emerged novel influenza strains through reassortment, avian influenza subtypes such as H5N1, H7N7, H7N2, H7N3 and H9N2 pose a constant threat in terms of their adaptation to the human host. Among these subtypes, it was recently demonstrated that mutations in H5 and H9 hemagglutinin (HA) in the context of lab-generated reassorted viruses conferred aerosol transmissibility in ferrets (a property shared by human adapted viruses). We previously demonstrated that the quantitative binding affinity of HA to α2→6 sialylated glycans (human receptors) is one of the important factors governing human adaptation of HA. Although the H7 subtype has infected humans causing varied clinical outcomes from mild conjunctivitis to severe respiratory illnesses, it is not clear where the HA of these subtypes stand in regard to human adaptation since its binding affinity to glycan receptors has not yet been quantified. In this study, we have quantitatively characterized the glycan receptor-binding specificity of HAs from representative strains of Eurasian (H7N7) and North American (H7N2) lineages that have caused human infection. Furthermore, we have demonstrated for the first time that two specific mutations; Gln226→Leu and Gly228→Ser in glycan receptor-binding site of H7 HA substantially increase its binding affinity to human receptor. Our findings contribute to a framework for monitoring the evolution of H7 HA to be able to adapt to human host.Karunya SrinivasanRahul RamanAkila JayaramanKarthik ViswanathanRam SasisekharanPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 2, p e49597 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Karunya Srinivasan Rahul Raman Akila Jayaraman Karthik Viswanathan Ram Sasisekharan Quantitative description of glycan-receptor binding of influenza A virus H7 hemagglutinin.
description	In the context of recently emerged novel influenza strains through reassortment, avian influenza subtypes such as H5N1, H7N7, H7N2, H7N3 and H9N2 pose a constant threat in terms of their adaptation to the human host. Among these subtypes, it was recently demonstrated that mutations in H5 and H9 hemagglutinin (HA) in the context of lab-generated reassorted viruses conferred aerosol transmissibility in ferrets (a property shared by human adapted viruses). We previously demonstrated that the quantitative binding affinity of HA to α2→6 sialylated glycans (human receptors) is one of the important factors governing human adaptation of HA. Although the H7 subtype has infected humans causing varied clinical outcomes from mild conjunctivitis to severe respiratory illnesses, it is not clear where the HA of these subtypes stand in regard to human adaptation since its binding affinity to glycan receptors has not yet been quantified. In this study, we have quantitatively characterized the glycan receptor-binding specificity of HAs from representative strains of Eurasian (H7N7) and North American (H7N2) lineages that have caused human infection. Furthermore, we have demonstrated for the first time that two specific mutations; Gln226→Leu and Gly228→Ser in glycan receptor-binding site of H7 HA substantially increase its binding affinity to human receptor. Our findings contribute to a framework for monitoring the evolution of H7 HA to be able to adapt to human host.
format	article
author	Karunya Srinivasan Rahul Raman Akila Jayaraman Karthik Viswanathan Ram Sasisekharan
author_facet	Karunya Srinivasan Rahul Raman Akila Jayaraman Karthik Viswanathan Ram Sasisekharan
author_sort	Karunya Srinivasan
title	Quantitative description of glycan-receptor binding of influenza A virus H7 hemagglutinin.
title_short	Quantitative description of glycan-receptor binding of influenza A virus H7 hemagglutinin.
title_full	Quantitative description of glycan-receptor binding of influenza A virus H7 hemagglutinin.
title_fullStr	Quantitative description of glycan-receptor binding of influenza A virus H7 hemagglutinin.
title_full_unstemmed	Quantitative description of glycan-receptor binding of influenza A virus H7 hemagglutinin.
title_sort	quantitative description of glycan-receptor binding of influenza a virus h7 hemagglutinin.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/499a621c49524985979546b90469b036
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Quantitative description of glycan-receptor binding of influenza A virus H7 hemagglutinin.

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