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Published on: January 7, 2019
Measles virus receptors
1Department of Virology, Faculty of Medicine, Kyushu University, 812-8582, Fukuoka, Japan. yyanagi@virology.med.kyushu-u.ac.jp
Abstract:
Measles virus (MV) has two envelope glycoproteins, the hemagglutinin (H) and fusion protein, which are responsible for attachment and membrane fusion, respectively. Signaling lymphocyte activation molecule (SLAM, also called CD150), a membrane glycoprotein expressed on immune cells, acts as the principal cellular receptor for MV, accounting for its lymphotropism and immunosuppressive nature. MV also infects polarized epithelial cells via an as yet unknown receptor molecule, thereby presumably facilitating transmission via aerosol droplets. Vaccine and laboratory-adapted strains of MV use ubiquitously expressed CD46 as an alternate receptor through amino acid substitutions in the H protein. The crystal structure of the H protein indicates that the putative binding sites for SLAM, CD46, and the epithelial cell receptor are strategically located in different positions of the H protein. Other molecules have also been implicated in MV infection, although their relevance remains to be determined. The identification of MV receptors has advanced our understanding of MV tropism and pathogenesis.
Insights
Measles virus (MV) uses immune cell receptors like Signaling Lymphocyte Activation Molecule (SLAM) and epithelial cell receptors for infection. Understanding these measles virus receptors is key to its tropism and pathogenesis.
Area of Science:
- Virology
- Immunology
- Structural Biology
Background:
- Measles virus (MV) possesses two envelope glycoproteins: hemagglutinin (H) and fusion protein, mediating attachment and membrane fusion.
- Signaling lymphocyte activation molecule (SLAM, CD150) is the primary receptor for MV on immune cells, driving lymphotropism and immunosuppression.
- MV infects epithelial cells via an unidentified receptor, potentially facilitating aerosol transmission, and utilizes CD46 as an alternative receptor in adapted strains.
Purpose of the Study:
- To elucidate the cellular receptors utilized by Measles virus (MV) for host cell entry.
- To understand the structural basis of MV receptor-ligand interactions.
- To advance the comprehension of MV tropism and pathogenesis through receptor identification.
Main Methods:
- Analysis of the crystal structure of the MV H protein.
- Implication of various molecules in MV infection.
- Comparative analysis of receptor binding sites on the H protein.
Main Results:
- The H protein's crystal structure reveals distinct binding sites for SLAM, CD46, and the epithelial cell receptor.
- SLAM is identified as the principal receptor for MV on immune cells.
- CD46 serves as an alternate receptor for vaccine and lab-adapted MV strains.
Conclusions:
- The identification of specific MV receptors (SLAM, CD46, and an unknown epithelial receptor) clarifies MV tropism.
- Structural insights into H protein interactions with receptors advance understanding of MV pathogenesis.
- Further research is needed to confirm the roles of other implicated molecules in MV infection.
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