Signaling lymphocyte activation molecule (SLAM) is thought to be a major cellular receptor for high-host specificity morbilliviruses, which cause devastating and highly infectious diseases in mammals. We determined the sequences of SLAM cDNA from five species of marine mammal, including two cetaceans, two pinnipeds and one sirenian, and generated three-dimensional models to understand the receptor-virus interaction. Twenty-one amino acid residues in the immunoglobulin-like V domains of the SLAMs were shown to bind the viral protein. Notably, the sequences from pinnipeds and dogs were highly homologous, which is consistent with the fact that canine distemper virus was previously shown to cause a mass die-off of seals. Among these twenty-one residues, eight (63, 66, 68, 72, 84, 119, 121 and 130) were shared by animal groups susceptible to a particular morbillivirus species. This set of residues appears to determine host-virus specificity and may be useful for risk estimation for morbilliviruses.

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