Amino acid sequence variations of signaling lymphocyte activation molecule and mortality caused by morbillivirus infection in cetaceans

• Published in: Microbiology and Immunology
• Main Authors: Shimizu, Yui, Ohishi, Kazue, Suzuki, Rintaro, Tajima, Yuko, Yamada, Tadasu, Kakizoe, Yuka, Bando, Takeharu, Fujise, Yoshihiro, Taru, Hajime, Murayama, Tsukasa, Maruyama, Tadashi
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2013
• Subjects: baleen whales
• Online Access: http://dx.doi.org/10.1111/1348-0421.12078; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2F1348-0421.12078; https://onlinelibrary.wiley.com/doi/pdf/10.1111/1348-0421.12078

ABSTRACT 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.