Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins

Abstract A(H3N2) influenza viruses have circulated in humans since 1968, and antigenic drift of the hemagglutinin (HA) protein continues to be a driving force that allows the virus to escape the human immune response. Since the major antigenic sites of the HA overlap into the receptor binding site (...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 2015-03, Vol.477, p.18-31
Main Authors: Yang, Hua, Carney, Paul J, Chang, Jessie C, Guo, Zhu, Villanueva, Julie M, Stevens, James
Format: Article
Language:English
Subjects:
Evolution, Molecular
Glycan microarray
H3N2
Hemagglutinin
Hemagglutinin Glycoproteins, Influenza Virus - genetics
Hemagglutinin Glycoproteins, Influenza Virus - metabolism
Humans
Infectious Disease
Influenza A Virus, H3N2 Subtype - genetics
Influenza A Virus, H3N2 Subtype - isolation & purification
Influenza A Virus, H3N2 Subtype - physiology
Influenza virus
Influenza, Human - virology
Mutant Proteins - genetics
Mutant Proteins - metabolism
Protein Binding
Receptor specificity
Receptors, Virus - metabolism
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Summary:Abstract A(H3N2) influenza viruses have circulated in humans since 1968, and antigenic drift of the hemagglutinin (HA) protein continues to be a driving force that allows the virus to escape the human immune response. Since the major antigenic sites of the HA overlap into the receptor binding site (RBS) of the molecule, the virus constantly struggles to effectively adapt to host immune responses, without compromising its functionality. Here, we have structurally assessed the evolution of the A(H3N2) virus HA RBS, using an established recombinant expression system. Glycan binding specificities of nineteen A(H3N2) influenza virus HAs, each a component of the seasonal influenza vaccine between 1968 and 2012, were analyzed. Results suggest that while its receptor-binding site has evolved from one that can bind a broad range of human receptor analogs to one with a more restricted binding profile for longer glycans, the virus continues to circulate and transmit efficiently among humans.
ISSN:0042-6822
1096-0341
DOI:10.1016/j.virol.2014.12.024