We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM.
- Authors
Hashiguchi, Takao; Ose, Toyoyuki; Kubota, Marie; Maita, Nobuo; Kamishikiryo, Jun; Maenaka, Katsumi; Yanagi, Yusuke
- 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.
- Subjects
MEASLES virus; HEMAGGLUTININ; MORTALITY; IMMUNOLOGIC diseases; ANTIVIRAL agents; CELL receptors; GLYCOPROTEINS; PARAMYXOVIRUSES; THERAPEUTICS
- Publication
Nature Structural & Molecular Biology, 2011, Vol 18, Issue 2, p135
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb.1969