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Conformational intermediates and fusion activity of influenza virus hemagglutinin

  1. Author:
    Korte, T.
    Ludwig, K.
    Booy, F. P.
    Blumenthal, R.
    Herrmann, A.

  2. Author Address

    Blumenthal R Humboldt Univ, Inst Biol Biophys, Math Nat Wissensch Fak 1 Invalidenstr 43 D-10115 Berlin Germany Humboldt Univ, Inst Biol Biophys, Math Nat Wissensch Fak 1 D-10115 Berlin Germany NCI, Frederick Canc Res & Dev Ctr, Lab Expt & Computat Biol, NIH Frederick, MD 21702 USA NIAMSD, NIH Bethesda, MD 20892 USA
    1. Year: 1999
  2. Journal: Journal of Virology
    1. 73
    2. 6
    3. Pages: 4567-4574
  4. Type of Article: Article
  1. Abstract:

    Three strains of influenza virus (H1, H2, and H3) exhibited similar characteristics in the ability of their hemagglutinin (HA) to induce membrane fusion, but the HAs differed in their susceptibility to inactivation. The extent of inactivation depended on the pH of preincubation and was lowest for A/Japan (H2 subtype), in agreement with previous studies (A, Purl, F. Booy, R. W. Doms, J, M, White, and R. Blumenthal, J, Virol, 64:3824-3832, 1990), While significant inactivation of X31 (H3 subtype) was observed at 37 degrees C at pH values corresponding to the maximum of fusion (about pH 5.0), no inactivation was seen at preincubation pH values 0.2 to 0.4 pH units higher. Surprisingly, low-pH preincubation under those conditions enhanced the fusion rates and extents of A/Japan as well as those of X31, For A/PR 8/34 (H1 subtype), neither a shift of the pH (to >5.0) nor a decrease of the temperature to 20 degrees C was sufficient to prevent inactivation, We provide evidence that the activated HA is a conformational intermediate distinct from the native structure and from the final structure associated with the conformational change of HA, which is implicated by the high-resolution structure of the soluble trimeric fragment TBHA2 (P, A. Bullough, F, M. Hughson, J, J, Skehel, and D. C. Wiley, Nature 371.:37-43, 1994). [References: 39]

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