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The heads of the measles virus attachment protein move to transmit the fusion-triggering signal.


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.

SUBMITTER: Navaratnarajah CK 

PROVIDER: S-EPMC3059746 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

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The heads of the measles virus attachment protein move to transmit the fusion-triggering signal.

Navaratnarajah Chanakha K CK   Oezguen Numan N   Rupp Levi L   Kay Leah L   Leonard Vincent H J VH   Braun Werner W   Cattaneo Roberto R  

Nature structural & molecular biology 20110109 2


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,  ...[more]

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