The heads of the measles virus attachment protein move to transmit the fusion-triggering signal
Identifieur interne : 001962 ( Istex/Curation ); précédent : 001961; suivant : 001963The heads of the measles virus attachment protein move to transmit the fusion-triggering signal
Auteurs : Chanakha K. Navaratnarajah [États-Unis] ; Numan Oezguen [États-Unis] ; Levi Rupp [États-Unis] ; Leah Kay [États-Unis] ; Vincent H J. Leonard [États-Unis] ; Werner Braun [États-Unis] ; Roberto Cattaneo [États-Unis]Source :
- Nature Structural & Molecular Biology [ 1545-9993 ] ; 2011-02.
Abstract
The measles virus entry system, consisting of attachment (hemagglutinin, H) and fusion proteins, operates by means of a variety of natural and targeted receptors; however, the mechanism that triggers fusion of the viral envelope with the plasma membrane is not understood. Here, we tested a model proposing that the two heads of an H dimer, which are covalently linked at their base, after binding two receptor molecules, move relative to each other to transmit the fusion-triggering signal. Indeed, stabilizing the H-dimer interface with additional intermolecular disulfide bonds prevented membrane fusion, an effect that was reversed by a reducing agent. Moreover, a membrane-anchored designated receptor efficiently triggered fusion, provided that it engaged the H dimer at locations proximal to where the natural receptors bind and distal to the H-dimer interface. We discuss how receptors may force H-protein heads to switch partners and transmit the fusion-triggering signal.
Url:
DOI: 10.1038/nsmb.1967
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<front><div type="abstract" xml:lang="eng">The measles virus entry system, consisting of attachment (hemagglutinin, H) and fusion proteins, operates by means of a variety of natural and targeted receptors; however, the mechanism that triggers fusion of the viral envelope with the plasma membrane is not understood. Here, we tested a model proposing that the two heads of an H dimer, which are covalently linked at their base, after binding two receptor molecules, move relative to each other to transmit the fusion-triggering signal. Indeed, stabilizing the H-dimer interface with additional intermolecular disulfide bonds prevented membrane fusion, an effect that was reversed by a reducing agent. Moreover, a membrane-anchored designated receptor efficiently triggered fusion, provided that it engaged the H dimer at locations proximal to where the natural receptors bind and distal to the H-dimer interface. We discuss how receptors may force H-protein heads to switch partners and transmit the fusion-triggering signal.</div>
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