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Title: Structure, Receptor Binding, and Antigenicity of Influenza Virus Hemagglutinins from the 1957 H2N2 Pandemic

Abstract

The hemagglutinin (HA) envelope protein of influenza viruses mediates essential viral functions, including receptor binding and membrane fusion, and is the major viral antigen for antibody neutralization. The 1957 H2N2 subtype (Asian flu) was one of the three great influenza pandemics of the last century and caused 1 million deaths globally from 1957 to 1968. Three crystal structures of 1957 H2 HAs have been determined at 1.60 to 1.75 {angstrom} resolutions to investigate the structural basis for their antigenicity and evolution from avian to human binding specificity that contributed to its introduction into the human population. These structures, which represent the highest resolutions yet recorded for a complete ectodomain of a glycosylated viral surface antigen, along with the results of glycan microarray binding analysis, suggest that a hydrophobicity switch at residue 226 and elongation of receptor-binding sites were both critical for avian H2 HA to acquire human receptor specificity. H2 influenza viruses continue to circulate in birds and pigs and, therefore, remain a substantial threat for transmission to humans. The H2 HA structure also reveals a highly conserved epitope that could be harnessed in the design of a broader and more universal influenza A virus vaccine.

Authors:
; ; ; ;  [1]
  1. Sinai
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1002292
Resource Type:
Journal Article
Journal Name:
J. Virol.
Additional Journal Information:
Journal Volume: 84; Journal Issue: (4) ; 02, 2010; Journal ID: ISSN 0022-538X
Country of Publication:
United States
Language:
ENGLISH
Subject:
36 MATERIALS SCIENCE; ANTIGENS; BIRDS; CRYSTAL STRUCTURE; DESIGN; ELONGATION; HEMAGGLUTININS; HUMAN POPULATIONS; INFLUENZA; INFLUENZA VIRUSES; MEMBRANES; PROTEINS; RESIDUES; SPECIFICITY

Citation Formats

Xu, Rui, McBride, Ryan, Paulson, James C, Basler, Christopher F, Wilson, Ian A, and Scripps). Structure, Receptor Binding, and Antigenicity of Influenza Virus Hemagglutinins from the 1957 H2N2 Pandemic. United States: N. p., 2010. Web. doi:10.1128/JVI.02162-09.
Xu, Rui, McBride, Ryan, Paulson, James C, Basler, Christopher F, Wilson, Ian A, & Scripps). Structure, Receptor Binding, and Antigenicity of Influenza Virus Hemagglutinins from the 1957 H2N2 Pandemic. United States. https://doi.org/10.1128/JVI.02162-09
Xu, Rui, McBride, Ryan, Paulson, James C, Basler, Christopher F, Wilson, Ian A, and Scripps). 2010. "Structure, Receptor Binding, and Antigenicity of Influenza Virus Hemagglutinins from the 1957 H2N2 Pandemic". United States. https://doi.org/10.1128/JVI.02162-09.
@article{osti_1002292,
title = {Structure, Receptor Binding, and Antigenicity of Influenza Virus Hemagglutinins from the 1957 H2N2 Pandemic},
author = {Xu, Rui and McBride, Ryan and Paulson, James C and Basler, Christopher F and Wilson, Ian A and Scripps)},
abstractNote = {The hemagglutinin (HA) envelope protein of influenza viruses mediates essential viral functions, including receptor binding and membrane fusion, and is the major viral antigen for antibody neutralization. The 1957 H2N2 subtype (Asian flu) was one of the three great influenza pandemics of the last century and caused 1 million deaths globally from 1957 to 1968. Three crystal structures of 1957 H2 HAs have been determined at 1.60 to 1.75 {angstrom} resolutions to investigate the structural basis for their antigenicity and evolution from avian to human binding specificity that contributed to its introduction into the human population. These structures, which represent the highest resolutions yet recorded for a complete ectodomain of a glycosylated viral surface antigen, along with the results of glycan microarray binding analysis, suggest that a hydrophobicity switch at residue 226 and elongation of receptor-binding sites were both critical for avian H2 HA to acquire human receptor specificity. H2 influenza viruses continue to circulate in birds and pigs and, therefore, remain a substantial threat for transmission to humans. The H2 HA structure also reveals a highly conserved epitope that could be harnessed in the design of a broader and more universal influenza A virus vaccine.},
doi = {10.1128/JVI.02162-09},
url = {https://www.osti.gov/biblio/1002292}, journal = {J. Virol.},
issn = {0022-538X},
number = (4) ; 02, 2010,
volume = 84,
place = {United States},
year = {Thu Mar 04 00:00:00 EST 2010},
month = {Thu Mar 04 00:00:00 EST 2010}
}