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

Yang H, Carney PJ, Chang JC, Guo Z, Villanueva JM, Stevens J
Virology 477 18-31 (2015)
Related entries: 4we4, 4we5, 4we6, 4we7, 4we9, 4wea

Cited: 75 times
EuropePMC logo PMID: 25617824

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.

Reviews - 4we8 mentioned but not cited (1)

  1. Biosensor-based epitope mapping of antibodies targeting the hemagglutinin and neuraminidase of influenza A virus. Guo Z, Wilson JR, York IA, Stevens J. J Immunol Methods 461 23-29 (2018)

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  2. H3N2 influenza viruses in humans: Viral mechanisms, evolution, and evaluation. Allen JD, Ross TM. Hum Vaccin Immunother 14 1840-1847 (2018)
  3. Sialylated Oligosaccharides and Glycoconjugates of Human Milk. The Impact on Infant and Newborn Protection, Development and Well-Being. Lis-Kuberka J, Orczyk-Pawiłowicz M. Nutrients 11 E306 (2019)
  4. Hemagglutinin Structure and Activities. Gamblin SJ, Vachieri SG, Xiong X, Zhang J, Martin SR, Skehel JJ. Cold Spring Harb Perspect Med 11 a038638 (2021)
  5. New insights into influenza A specificity: an evolution of paradigms. Ji Y, White YJ, Hadden JA, Grant OC, Woods RJ. Curr Opin Struct Biol 44 219-231 (2017)
  6. Influence of Host Sialic Acid Receptors Structure on the Host Specificity of Influenza Viruses. Zhao C, Pu J. Viruses 14 2141 (2022)
  7. Glycomics and glycoproteomics of viruses: Mass spectrometry applications and insights toward structure-function relationships. Cipollo JF, Parsons LM. Mass Spectrom Rev 39 371-409 (2020)
  8. Antivirals Targeting the Neuraminidase. Gubareva L, Mohan T. Cold Spring Harb Perspect Med 12 a038455 (2022)
  9. Co-evolution of immunity and seasonal influenza viruses. Han AX, de Jong SPJ, Russell CA. Nat Rev Microbiol 21 805-817 (2023)
  10. Identification and Characteristics of Fusion Peptides Derived From Enveloped Viruses. Lozada C, Barlow TMA, Gonzalez S, Lubin-Germain N, Ballet S. Front Chem 9 689006 (2021)
  11. A changing trend in diagnostic methods of Influenza A (H3N2) virus in human: a review. Ravina, Manjeet, Mohan H, Narang J, Pundir S, Pundir CS. 3 Biotech 11 87 (2021)

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