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Hemagglutinin Structure and Activities.

Gamblin SJ, Vachieri SG, Xiong X, Zhang J, Martin SR, Skehel JJ
Cold Spring Harb Perspect Med 11 (2021)
Cited: 13 times
EuropePMC logo PMID: 32513673

Abstract

Hemagglutinins (HAs) are the receptor-binding and membrane fusion glycoproteins of influenza viruses. They recognize sialic acid-containing, cell-surface glycoconjugates as receptors but have limited affinity for them, and, as a consequence, virus attachment to cells requires their interaction with several virus HAs. Receptor-bound virus is transferred into endosomes where membrane fusion by HAs is activated at pH between 5 and 6.5, depending on the strain of virus. Fusion activity requires extensive rearrangements in HA conformation that include extrusion of a buried "fusion peptide" to connect with the endosomal membrane, form a bridge to the virus membrane, and eventually bring both membranes close together. In this review, we give an overview of the structures of the 16 genetically and antigenically distinct subtypes of influenza A HA in relation to these two functions in virus replication and in relation to recognition of HA by antibodies that neutralize infection.

Reviews citing this publication (4)

  1. Influenza and Universal Vaccine Research in China. Li J, Zhang Y, Zhang X, Liu L. Viruses 15 116 (2022)
  2. Subdominance in Antibody Responses: Implications for Vaccine Development. Lindahl G. Microbiol Mol Biol Rev 85 e00078-20 (2020)
  3. Influence of Host Sialic Acid Receptors Structure on the Host Specificity of Influenza Viruses. Zhao C, Pu J. Viruses 14 2141 (2022)
  4. Quinones as Promising Compounds against Respiratory Viruses: A Review. Chan-Zapata I, Borges-Argáez R, Ayora-Talavera G. Molecules 28 1981 (2023)

Articles citing this publication (9)

  1. S-Acylation of Proteins of Coronavirus and Influenza Virus: Conservation of Acylation Sites in Animal Viruses and DHHC Acyltransferases in Their Animal Reservoirs. Abdulrahman DA, Meng X, Veit M. Pathogens 10 669 (2021)
  2. Message in a bottle: mRNA vaccination for influenza. Shartouny JR, Lowen AC. J Gen Virol 103 (2022)
  3. Self-amplifying mRNA bicistronic influenza vaccines raise cross-reactive immune responses in mice and prevent infection in ferrets. Chang C, Music N, Cheung M, Rossignol E, Bedi S, Patel H, Safari M, Lee C, Otten GR, Settembre EC, Palladino G, Wen Y. Mol Ther Methods Clin Dev 27 195-205 (2022)
  4. Characterization of changes in the hemagglutinin that accompanied the emergence of H3N2/1968 pandemic influenza viruses. West J, Röder J, Matrosovich T, Beicht J, Baumann J, Mounogou Kouassi N, Doedt J, Bovin N, Zamperin G, Gastaldelli M, Salviato A, Bonfante F, Kosakovsky Pond S, Herfst S, Fouchier R, Wilhelm J, Klenk HD, Matrosovich M. PLoS Pathog 17 e1009566 (2021)
  5. Global Infection Rate of Rotavirus C during 1980-2022 and Analysis of Critical Factors in the Host Range Restriction of Virus VP4. Zhao S, Jin X, Zang L, Liu Z, Wen X, Ran X. Viruses 14 2826 (2022)
  6. Effects of Receptor Specificity and Conformational Stability of Influenza A Virus Hemagglutinin on Infection and Activation of Different Cell Types in Human PBMCs. Dorna J, Kaufmann A, Bockmann V, Raifer H, West J, Matrosovich M, Bauer S. Front Immunol 13 827760 (2022)
  7. Mechanistic dissection of antibody inhibition of influenza entry yields unexpected heterogeneity. Sengar A, Cervantes M, Kasson PM. Biophys J 122 1996-2006 (2023)
  8. H3N2 influenza A virus gradually adapts to human-type receptor binding and entry specificity after the start of the 1968 pandemic. Liu M, Bakker AS, Narimatsu Y, van Kuppeveld FJM, Clausen H, de Haan CAM, de Vries E. Proc Natl Acad Sci U S A 120 e2304992120 (2023)
  9. Palmitoylation of the hemagglutinin of influenza B virus by ER-localized DHHC enzymes 1, 2, 4, and 6 is required for efficient virus replication. Meng X, Veit M. J Virol 97 e0124523 (2023)


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