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. 1986 Jan;5(1):41-9.
doi: 10.1002/j.1460-2075.1986.tb04175.x.

Electron microscopy of the low pH structure of influenza virus haemagglutinin

R W Ruigrok, N G Wrigley, L J Calder, S Cusack, S A Wharton, E B Brown, J J Skehel

Electron microscopy of the low pH structure of influenza virus haemagglutinin

R W Ruigrok et al. EMBO J. 1986 Jan.

Abstract

Influenza virus haemagglutinin mediates infection of cells by fusion of viral and endosomal membranes, triggered by low pH which induces a conformational change in the protein. We report studies of this change by electron microscopy, neutron scattering, sedimentation and photon correlation on X-31 (H3N2) haemagglutinin, both intact and bromelain cleaved, in various assemblies. HAs in all preparations showed a thinning at low pH, and a marked elongation which was removed on tryptic digestion, revealing altered features in the remaining stem portion of the molecule. A tentative model of the change is proposed, with reference to the known X-ray structure at neutral pH, in which major changes occur in the stem tertiary structure, while the top portion is only affected in its quaternary structure.

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