M Khosravi - Department of Pathobiology, Faculty of Veterinary Medicine, Amol University of Special of Modern Technologies, Amol, Iran
F Mohammdzadeh - BSc Student in Veterinary Laboratory Sciences, Department of Pathobiology, Faculty of Veterinary Medicine,Amol University of Special of Modern Technologies, Amol, Iran

Morbilliviruses are single-stranded RNA viruses that belong to the Paramyxoviridae family,including several deadly human and animal infecting viruses. The first step of virus-cell entry has beenpromoting through the interaction between hemagglutinin protein (H) and cellular receptors via its headdomain. Up to now, signaling lymphocyte activation molecule (SLAM) and Nectin-۴ are recognized ascellular receptors. Morbilliviruses could develop CNS disorders and no receptor has been introducedfor nerves cells “[۱]”. The prior findings revealed that relatively same region of the head domain isassociated with cellular receptor interaction. This study is designed to find potential region of headdomain involving to novel cellular receptor interaction. For this reason, alignment analysis at aminoacid level was conducted among several reference strains of morbillivirus. Our result showed that fivenearly conserved regions designed as A,B,C,E and D. The E region (۵۱۲ to ۵۴۳ aa) is associated withthe both SLAM and Nectin-۴ receptors “[۲]”. Furthermore, ۳D structure measles H protein and humanSLAM revealed that regions A and D are situated upon the protein's surface. Additionally, these tworegions contain several highly conserved residues and also offer a relatively suitable surface forinteracting with the novel receptor. By considering with the pattern exhibited by the H protein in relationto previously recognized receptors, it can be concluded that H protein may employ a comparable patternor alternatively share distinct region to bind the new receptor. Further biochemical studies at the in vitrolevel are highly recommended to substantiate this matter.

Morbillivirus; H portion; slam; nectin-۴; novel receptor