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

• HASHIGUCHI T

抄録

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.

収録刊行物

• Nature Structural & Molecular Biology

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

  Nature Pablishing Group

詳細情報

• CRID: 1571135651475567488
• NII論文ID: 80021640608
• NII書誌ID: AA10987726
• ISSN: 10728368
• DOI: 10.1038/nsmb.1969
• Web Site: http://hdl.handle.net/2324/19802
• 本文言語コード: en
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