Identification of key residues in virulent canine distemper virus hemagglutinin that control CD150/SLAM-binding activity.
Morbillivirus cell entry is controlled by hemagglutinin (H), an envelope-anchored viral glycoprotein determining interaction with multiple host cell surface receptors. Subsequent to virus-receptor attachment, H is thought to transduce a signal triggering the viral fusion glycoprotein, which in turn drives virus-cell fusion activity. Cell entry through the universal morbillivirus receptor CD150/SLAM was reported to depend on two nearby microdomains located within the hemagglutinin. Here, we provide evidence that three key residues in the virulent canine distemper virus A75/17 H protein (Y525, D526, and R529), clustering at the rim of a large recessed groove created by beta-propeller blades 4 and 5, control SLAM-binding activity without drastically modulating protein surface expression or SLAM-independent F triggering.
Zipperle
Ljerka
L
Department of Clinical Research and Veterinary Public Health, Vetsuisse Faculty, University of Bern, Bern, Switzerland.
Langedijk
Johannes P M
JP
Orvell
Claes
C
Vandevelde
Marc
M
Zurbriggen
Andreas
A
Plattet
Philippe
P
D000818:Animals; D015703:Antigens, CD / Q000378:metabolism*; D002522:Chlorocebus aethiops; D004217:Distemper Virus, Canine / Q000235:genetics / Q000502:physiology*; D004285:Dogs; D006389:Hemagglutinins, Viral / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011991:Receptors, Virus / Q000378:metabolism*; D000071177:Signaling Lymphocytic Activation Molecule Family Member 1; D014709:Vero Cells; D053585:Virus Attachment
D015703:Antigens, CD; D006389:Hemagglutinins, Viral; D011956:Receptors, Cell Surface; D011991:Receptors, Virus; D000071177:Signaling Lymphocytic Activation Molecule Family Member 1