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ph-Dependent hydrophobicity profile of hemagglutinin of influenza virus and its possible relevance in virus fusion

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Abstract

The hydropathy profile of hemagglutinin (HA) subunits HA1 and HA2 of influenza virus X31 and A/PR 8/34 is analyzed at different pH. At neutral pH (7.4) pronounced hydrophobic sequences of HA correspond to the N-terminus and the transmembrane spanning sequence of HA2. At pH 5.0 where influenza virus is known to fuse with biological membranes several hydrophobic sequences in the ectodomain exist which are comparable in both the hydrophobicity and length of the N-terminus of HA2. It is suggested that these hydrophobic stretches are important for the fusion complex, in addition to the N-terminal site of HA2.

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Abbreviations

HA:

hemagglutinin

NHA2:

N-terminus of HA2

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Authors and Affiliations

  1. Fachbereich Biologie, Institut für Biophysik, Humboldt-Universität zu Berlin, Invalidenstr. 42, D-O-1040, Berlin, Germany

    Thomas Korte, Kai Ludwig & Andreas Herrmann

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  1. Thomas Korte
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  2. Kai Ludwig
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  3. Andreas Herrmann
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Korte, T., Ludwig, K. & Herrmann, A. ph-Dependent hydrophobicity profile of hemagglutinin of influenza virus and its possible relevance in virus fusion. Biosci Rep 12, 397–406 (1992). https://doi.org/10.1007/BF01121503

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  • DOI: https://doi.org/10.1007/BF01121503

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