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.
Highlights
Morbilliviruses belong to the genus Morbillivirus and the family Paramyxoviridae
signaling lymphocyte activation molecule (SLAM) residues are seemingly important for interaction with the morbillivirus H protein and form the binding interface [30,151]
Because cetacean morbillivirus (CeMV) infects a broad range of cetacean species, its H
Summary
Morbilliviruses belong to the genus Morbillivirus and the family Paramyxoviridae. Morbillivirus species have high host specificity and infection results in a highly contagious and devastating disease [1]. 1980s and 1990s from dead seals or cetaceans from mass-die-offs or strandings, and named phocine distemper virus (PDV; phocine morbillivirus) and cetacean morbillivirus (CeMV) [2,3,4,5,6] In addition to these six well-known species, novel morbilliviruses have been identified in domestic cats and bats [7,8]. The amino acid sequences of SLAMs are more divergent among host species [29,30] compared with those of nectin-4, which are highly conserved [31,32] This suggests that SLAM plays a greater role than nectin-4 in determining the host specificity of morbilliviruses. Recent epidemiological findings of marine morbilliviruses are described from the viewpoint of the interaction between viruses and their major host cell receptor, SLAM
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