Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Original publication

DOI

10.1098/rstb.2014.0034

Type

Journal article

Journal

Philos Trans R Soc Lond B Biol Sci

Publication Date

05/02/2015

Volume

370

Keywords

W. G. Laver, crystallography, influenza, neuraminidase, sialic acid, Antiviral Agents, History, 20th Century, Humans, Influenza A virus, Influenza, Human, Neuraminidase, Receptors, Cell Surface