Cell entry by measles virus: Long hybrid receptors uncouple binding from membrane fusion

Christian J. Buchholz, Urs Schneider, Patricia Devaux, Denis Gerlier, Roberto Cattaneo

Research output: Contribution to journalArticlepeer-review

63 Scopus citations


The pH-independent fusion of membranes induced by measles virus (MV) requires, in addition to the fusion-competent protein F, hemagglutinin (H), and on the target membrane, the virus receptor CD46. We constructed hybrid receptors composed of different numbers and combinations of the four CD46 short consensus repeat (SCR) domains, followed by immunoglobulin-like domains of another cell surface protein, CD4. Hybrid proteins containing SCRs I and II bound MV particles and conferred fusion competence to rodent cells. SCRs III and/or IV strengthened MV binding. Increasing the distance between the MV binding site and the transmembrane domain enhanced virus binding but reduced fusion efficiency. A hybrid protein predicted to be about 120 Å (12 nm) longer than the standard receptor lost fusion support function and was dominant negative over a functional receptor. These data indicate that receptor protein length influences virus binding and determines fusion efficiency.

Original languageEnglish (US)
Pages (from-to)3716-3723
Number of pages8
JournalJournal of virology
Issue number6
StatePublished - 1996

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology


Dive into the research topics of 'Cell entry by measles virus: Long hybrid receptors uncouple binding from membrane fusion'. Together they form a unique fingerprint.

Cite this