Conformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: effects of acid pretreatment (Q27486597)

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F P Booy

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R W Doms

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J M White

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R Blumenthal

The structure and function of the hemagglutinin membrane glycoprotein of influenza virus

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publication date

August 1990

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published in

Journal of Virology

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volume

64

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issue

8

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page(s)

3824-32

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cites work

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Cloning and DNA sequence of double-stranded copies of haemagglutinin genes from H2 and H3 strains elucidates antigenic shift and drift in human influenza virus

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Membrane fusion activity of influenza virus.

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Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion

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Hemolytic activity of influenza virus hemagglutinin glycoproteins activated in mildly acidic environments

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Monoclonal anti-hemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A/PR/834-mediated hemolysis

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Fluorescence method for measuring the kinetics of fusion between biological membranes

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Electron microscopy of the low pH structure of influenza virus haemagglutinin

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Human immunodeficiency virus infection of CD4-bearing cells occurs by a pH-independent mechanism

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Kinetics of pH-dependent fusion between 3T3 fibroblasts expressing influenza hemagglutinin and red blood cells. Measurement by dequenching of fluorescence

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Activation of vesicular stomatitis virus fusion with cells by pretreatment at low pH.

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Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin

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Membrane fusion activity of the influenza virus hemagglutinin. The low pH-induced conformational change.

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Effects of low pH on influenza virus. Activation and inactivation of the membrane fusion capacity of the hemagglutinin

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27 November 2018

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27 November 2018

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