Identification of key residues in virulent canine distemper virus hemagglutinin that control CD150/SLAM-binding activity.

摘要: Morbillivirus cell entry is controlled by hemagglutinin (H), an envelope-anchored viral glycoprotein determining interaction with multiple host surface receptors. Subsequent to virus-receptor attachment, H thought transduce a signal triggering the fusion glycoprotein, which in turn drives virus-cell activity. Cell through universal morbillivirus receptor CD150/SLAM was reported depend on two nearby microdomains located within hemagglutinin. Here, we provide evidence that three key residues virulent canine distemper virus A75/17 protein (Y525, D526, and R529), clustering at rim of large recessed groove created β-propeller blades 4 5, control SLAM-binding activity without drastically modulating expression or SLAM-independent F triggering.