Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin.

By J. Skehel, D. Wiley. Annual Review of Biochemistry, 2000

2,816 citations recorded by the source corpus.

Subfields: Epidemiology, Genetics, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/956e7739221918004f96d5722e71e96e37499eaf

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Citations in the corpus

New World Bats Harbor Diverse Influenza A Viruses (2013, background): “The RBS in influenza A contains several highly conserved amino acids at its base: Tyr98, Trp153, His183, and Tyr195 (H3 numbering, Tables S3 and S8), and three major structural elements at its edge: 130-loop (134–138), 220-loop (221– 228), and 190-helix (188–194) [16,17].”
Distinct Patterns of IFITM-Mediated Restriction of Filoviruses, SARS Coronavirus, and Influenza A Virus (2011, background): “The conformational changes of some entry proteins, for example IAV HA or flavivirus E proteins, are induced by low pH [7,8].”
Glycan repositioning of influenza hemagglutinin stem facilitates the elicitation of protective cross-group antibody responses (2020, background): “Hemagglutinin (HA) is the most prevalent influenza viral surface glycoprotein and engages sialic acid moieties on host cell surface to mediate viral attachment, virus-host membrane fusion and infection 1, 2 .”
The Biogenesis and Functions of Exosomes (2002, background): “Virus fusion with the endosomal membrane has been described best for influenza virus (89).”
Design and development of polymers for gene delivery (2005, background): “Many viruses have evolved specific acidic peptide sequences in their protein coat that are protonated at acidic pH and become fusogenic with the endosomal membrane, enabling delivery of their DNA or RNA cargo directly into the cytoplas”
Sialic acids in the brain: gangliosides and polysialic acid in nervous system development, stability, disease, and regeneration. (2014, background): “This was first discovered in the study of pathogens that evolved to bind to these abundant and readily accessible cell surface targets (259), of which influenza viruses are the best studied (338, 450, 462).”
Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common Theme (2008, background): “The pH at which these conformational changes are triggered varies for different strains of influenza virus, and many mutations have been described that alter the pH dependence of fusion (Rachakonda et al., 2007; Skehel and Wiley, 2000; Thoennes et al., 2007).”
Structural and Functional Bases for Broad-Spectrum Neutralization of Avian and Human Influenza A Viruses (2009, neutral): “nAbs inhibit cell fusion rather than receptor binding Two ways in which anti-hemagglutinin antibodies can neutralize infection is by blocking the initial binding of hemagglutinin to its cellular receptor (sialic acid) or by interfering with the subsequent step of hemagglutinin-mediated virus-host”
Next-Generation Influenza Vaccines. (2020, background): “HA engages sialosides on host glycoproteins and glycolipids through its receptorbinding site located on the membrane distal, globular head domain (Skehel and Wiley 2000; de Graaf and Fouchier 2014).”