H2N2V1, Main, Exploration, bibRecord, 001F43

Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity

Identifieur interne : 001F43 ( Main/Exploration ); précédent : 001F42; suivant : 001F44

Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity

Auteurs : L. Godley [États-Unis] ; J. Pfeifer [États-Unis] ; D. Steinhauer ; B. Ely ; G. Shaw [États-Unis] ; R. Kaufmann [États-Unis] ; E. Suchanek [États-Unis] ; C. Pabo [États-Unis] ; J. J. Skehel ; D. C. Wiley [États-Unis] ; S. Wharton

Source :

Cell [ 0092-8674 ] ; 1992.

RBID : ISTEX:9801974B5F60FC8F784C5085156C8484E102CC0F

English descriptors

Teeft :
- Alkylated, Alkylation, Amino, Amino acid substitutions, Amino terminus, Assay, Cell lysate, Cell lysates, Cell surface, Conformation, Conformational, Conformational change, Conformational changes, Digestion, Disulfide, Disulfide bonds, Electron microscopy, Fetal calf serum, Fusion, Fusion activity, Fusion peptide, Haemagglutinin, Hemagglutinin, Hemolysis, Immunoprecipitated, Influenza, Influenza virus, Influenza virus haemagglutinin, Influenza virus hemagglutinin, Inhibitor, Intersubunit, Intersubunit disulfide bonds, Iodoacetamide, Lysates, Membrane, Membrane fusion, Membrane fusion activity, Molecular weight, Molecular weights, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Mutant, Mutant cells, Nonreducing conditions, Novel disulfide bonds, Polypeptide, Posttranslational modifications, Receptor binding, Skehel, Structural changes, Subunit, Sucrose, Trimer, Trypsin, Trypsin cleavage, Trypsin inhibitor, Trypsin treatment, Viral, Wharton, Wild type.

Abstract

Abstract: Influenza virus hemagglutinin (HA) mediates viral entry into cells by a low pH-induced membrane fusion event in endosomes. A number of structural changes occur throughout the length of HA at the pH of fusion. To probe their significance and their necessity for fusion activity, we have prepared a site-directed mutant HA containing novel intersubunit disulfide bonds designed to cross-link covalently the membrane-distal domains of the trimer. These mutations inhibited the low pH-induced conformational changes and prevented HA-mediated membrane fusion; conditions that reduced the novel disulfide bonds restored membrane fusion activity. We conclude that structural rearrangements in the membrane distal region of the HA are required for membrane fusion activity.

Url:

https://api.istex.fr/ark:/67375/6H6-L06513WM-3/fulltext.pdf

DOI: 10.1016/0092-8674(92)90140-8

Affiliations:

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Le document en format XML

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<term>Haemagglutinin</term>
<term>Hemagglutinin</term>
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<term>Immunoprecipitated</term>
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<term>Influenza virus</term>
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<front><div type="abstract" xml:lang="en">Abstract: Influenza virus hemagglutinin (HA) mediates viral entry into cells by a low pH-induced membrane fusion event in endosomes. A number of structural changes occur throughout the length of HA at the pH of fusion. To probe their significance and their necessity for fusion activity, we have prepared a site-directed mutant HA containing novel intersubunit disulfide bonds designed to cross-link covalently the membrane-distal domains of the trimer. These mutations inhibited the low pH-induced conformational changes and prevented HA-mediated membrane fusion; conditions that reduced the novel disulfide bonds restored membrane fusion activity. We conclude that structural rearrangements in the membrane distal region of the HA are required for membrane fusion activity.</div>
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Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity

Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity

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English descriptors

Abstract

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