ph-dependent hydrophobicity profile of hemagglutinin of influenza virus and its possible relevance in virus fusion.
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.
Korte
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T
Humboldt-Universität zu Berlin, Fachbereich Biologie, Institut für Biophysik, Germany.
Ludwig
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K
Herrmann
A
A
D006388:Hemagglutinins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D009975:Orthomyxoviridae / Q000737:chemistry*; D014760:Viral Fusion Proteins / Q000737:chemistry*
D006388:Hemagglutinins; D014760:Viral Fusion Proteins