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

Takao Hashiguchi, Toyoyuki Ose, Marie Kubota, Nobuo Maita, Jun Kamishikiryo, Katsumi Maenaka, Yusuke Yanagi

Research output: Contribution to journalArticle

148 Citations (Scopus)

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 β-sheet of the membrane-distal ectodomain of SLAM using the side of its β-propeller fold. This is distinct from attachment proteins of other paramyxoviruses that bind receptors using the top of their β-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.

Original languageEnglish
Pages (from-to)135-142
Number of pages8
JournalNature Structural and Molecular Biology
Volume18
Issue number2
DOIs
Publication statusPublished - Feb 2011

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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