Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM

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Abstract

Measles virus, a major cause of childhood morbidity and mortality worldwide, predominantly infects immune cells using signaling lymphocyte activation molecule (SLAM) as a cellular receptor. Here we present crystal structures of measles virus hemagglutinin (MV-H), the receptor-binding glycoprotein, in complex with SLAM. The MV-H head domain binds to a b-sheet of the membrane-distal ectodomain of SLAM using the side of its b-propeller fold. This is distinct from attachment proteins of other paramyxoviruses that bind receptors using the top of their b-propeller. The structure provides templates for antiviral drug design, an explanation for the effectiveness of the measles virus vaccine, and a model of the homophilic SLAM-SLAM interaction involved in immune modulations. Notably, the crystal structures obtained show two forms of the MV-H–SLAM tetrameric assembly (dimer of dimers), which may have implications for the mechanism of fusion triggering.

Journal

  • Nature Structural & Molecular Biology

    Nature Structural & Molecular Biology 18(2), 135-141, 2011-02

    Nature Pablishing Group

Cited by:  1

Codes

  • NII Article ID (NAID)
    80021640608
  • NII NACSIS-CAT ID (NCID)
    AA10987726
  • Text Lang
    ENG
  • Article Type
    Journal Article
  • ISSN
    1072-8368
  • Data Source
    CJPref  IR 
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