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  • Title: Electron microscopy of the low pH structure of influenza virus haemagglutinin.
    Author: Ruigrok RW, Wrigley NG, Calder LJ, Cusack S, Wharton SA, Brown EB, Skehel JJ.
    Journal: EMBO J; 1986 Jan; 5(1):41-9. PubMed ID: 3956479.
    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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