Conformational change of influenza virus hemagglutinin is sensitive to ionic concentration |
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Authors: | Thomas Korte Kai Ludwig Qiang Huang P Sivaramakrishna Rachakonda Andreas Herrmann |
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Institution: | (1) Institute of Biology, Molecular Biophysics, Humboldt University, Invalidenstr. 42, Berlin, 10115, Germany;(2) Research Center for Electron Microscopy, Free University Berlin, Fabeckstr. 36a, Berlin, 14195, Germany;(3) State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai, 200433, China |
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Abstract: | The homotrimeric spike glycoprotein hemagglutinin (HA) of influenza virus undergoes a low pH-mediated conformational change
which mediates the fusion of the viral envelope with the target membrane. Previous approaches predict that the interplay of
electrostatic interactions between and within HA subunits, HA 1 and HA2, are essential for the metastability of the HA ectodomain.
Here, we show that suspension media of low ionic concentration promote fusion of fluorescent labelled influenza virus X31
with erythrocyte ghosts and with ganglioside containing liposomes. By measuring the low pH mediated inactivation of the fusion
competence of HA and the Proteinase K sensitivity of low pH incubated HA we show that the conformational change is promoted
by low ionic concentration. We surmise that electrostatic attraction within the HA ectodomain is weakened by lowering the
ionic concentration facilitating the conformational change at low pH.
Dedicated to Prof. K. Arnold on the occasion of his 65th birthday. |
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Keywords: | Influenza virus Hemagglutinin Fusion Ionic concentration Fluorescence |
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