e-journal
Amino acid sequence variations of signaling lymphocyte activation molecule and mortality caused by morbillivirus infection in cetaceans
Morbillivirus infection is a severe threat to marine mammals.Mass die‐offs caused by this infection have
repeatedly occurred in bottlenose dolphins (Turiops truncatus) and striped dolphins (Stenella
coeruleoalba), both of which belong to the family Delphinidae, but not in other cetaceans. However,
it is unknown whether sensitivity to the virus varies among cetacean species. The signaling lymphocyte
activation molecule (SLAM) is a receptor on host cells that allows morbillivirus invasion and
propagation. Its immunoguloblin variable domain‐like (V) region provides an interface for the virus
hemagglutinin (H) protein. In this study, variations in the amino acid residues of the V region of
26 cetacean species, covering almost all cetacean genera, were examined. Three‐dimensional (3D) models
of them were generated in a homology model using the crystal structure of the marmoset SLAM and
measles virus H protein complex as a template. The 3D models showed 32 amino acid residues on the
interface that possibly bind the morbillivirus. Among the cetacean species studied, variations were found
at six of the residues. Bottlenose and striped dolphins have substitutions at five positions (E68G, I74V,
R90H, V126I, and Q130H) compared with those of baleen whales. Three residues (at positions 68, 90 and
130) were found to alternate electric charges, possibly causing changes in affinity for the virus. This study
shows a new approach based on receptor structure for assessing potential vulnerability to viral infection.
This method may be useful for assessing the risk of morbillivirus infection in wildlife.
Key words cetacean, morbillivirus, receptor, signaling lymphocyte activation molecule.
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