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Published on: June 29, 2016
Marine Morbilliviruses: Diversity and Interaction with Signaling Lymphocyte Activation Molecules
Kazue Ohishi1, Tadashi Maruyama2, Fumio Seki3
1Faculty of Engineering, Tokyo Polytechnic University, 1583, Iiyama, Atsugi, Kanagawa 243-0297, Japan. cie20910@syd.odn.ne.jp.
Abstract:
Epidemiological reports of phocine distemper virus (PDV) and cetacean morbillivirus (CeMV) have accumulated since their discovery nearly 30 years ago. In this review, we focus on the interaction between these marine morbilliviruses and their major cellular receptor, the signaling lymphocyte activation molecule (SLAM). The three-dimensional crystal structure and homology models of SLAMs have demonstrated that 35 residues are important for binding to the morbillivirus hemagglutinin (H) protein and contribute to viral tropism. These 35 residues are essentially conserved among pinnipeds and highly conserved among the Caniformia, suggesting that PDV can infect these animals, but are less conserved among cetaceans. Because CeMV can infect various cetacean species, including toothed and baleen whales, the CeMV-H protein is postulated to have broader specificity to accommodate more divergent SLAM interfaces and may enable the virus to infect seals. In silico analysis of viral H protein and SLAM indicates that each residue of the H protein interacts with multiple residues of SLAM and vice versa. The integration of epidemiological, virological, structural, and computational studies should provide deeper insight into host specificity and switching of marine morbilliviruses.
Insights
Marine morbilliviruses like phocine distemper virus (PDV) and cetacean morbillivirus (CeMV) interact with the SLAM receptor. Understanding these interactions is key to predicting viral host specificity and potential host switching events.
Area of Science:
- Marine virology
- Immunology
- Structural biology
Background:
- Phocine distemper virus (PDV) and cetacean morbillivirus (CeMV) are marine morbilliviruses with significant epidemiological impact.
- The signaling lymphocyte activation molecule (SLAM) is the primary cellular receptor for these viruses.
Purpose of the Study:
- To review the interaction between marine morbilliviruses (PDV and CeMV) and their cellular receptor, SLAM.
- To elucidate the structural basis of viral tropism and host specificity.
Main Methods:
- Analysis of three-dimensional crystal structures and homology models of SLAM.
- In silico analysis of viral hemagglutinin (H) protein and SLAM interactions.
- Integration of epidemiological, virological, structural, and computational data.
Main Results:
- 35 key residues in SLAM are crucial for binding the morbillivirus H protein and determining viral tropism.
- These residues are highly conserved in pinnipeds, suggesting PDV's potential to infect them.
- Less conserved SLAM residues in cetaceans suggest broader CeMV-H protein specificity for infecting diverse whale species and potentially seals.
Conclusions:
- SLAM-morbillivirus H protein interactions are critical for host specificity.
- Structural and computational analyses reveal complex residue interactions governing viral tropism.
- Integrating diverse study types offers insights into marine morbillivirus host switching.
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