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

  • Zipperle L
  • Langedijk J
  • Orvell C
 et al. 
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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.

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  • Ljerka Zipperle

  • Johannes P M Langedijk

  • Claes Orvell

  • Marc Vandevelde

  • Andreas Zurbriggen

  • Philippe Plattet

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