title: Antiviral adhesion molecular mechanisms for influenza: W. G. Laver's lifetime obsession.
abstract: Infection by the influenza virus depends firstly on cell adhesion via the sialic-acid-binding viral surface protein, haemagglutinin, and secondly on the successful escape of progeny viruses from the host cell to enable the virus to spread to other cells. To achieve the latter, influenza uses another glycoprotein, the enzyme neuraminidase (NA), to cleave the sialic acid receptors from the surface of the original host cell. This paper traces the development of anti-influenza drugs, from the initial suggestion by MacFarlane Burnet in 1948 that an effective 'competitive poison' of the virus' NA might be useful in controlling infection by the virus, through to the determination of the structure of NA by X-ray crystallography and the realization of Burnet's idea with the design of NA inhibitors. A focus is the contribution of the late William Graeme Laver, FRS, to this research.
authors.affiliation: Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK elspeth.garman@bioch.ox.ac.uk.
authors.forename: Elspeth F
authors.initials: EF
authors.lastname: Garman
mesh_terms: D000998:Antiviral Agents / Q000266:history / Q000494:pharmacology*; D049673:History, 20th Century; D006801:Humans; D009980:Influenza A virus / Q000187:drug effects* / Q000502:physiology; D007251:Influenza, Human / Q000188:drug therapy*; D009439:Neuraminidase / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000502:physiology
chemical_list: D000998:Antiviral Agents; D011956:Receptors, Cell Surface; C092488:sialic acid receptor; D009439:Neuraminidase
keywords: W. G. Laver; crystallography; influenza; neuraminidase; sialic acid