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

Chanakha K. Navaratnarajah, Numan Oezguen, Levi Rupp, Leah Kay, Vincent H.J. Leonard, Werner Braun, Roberto Cattaneo

Research output: Contribution to journalArticle

81 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)128-135
Number of pages8
JournalNature Structural and Molecular Biology
Issue number2
StatePublished - Feb 1 2011


ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this