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

  • Zipperle L
  • Langedijk J
  • Orvell C
 et al. 
  • 19

    Readers

    Mendeley users who have this article in their library.
  • 23

    Citations

    Citations of this article.

Abstract

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.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • Ljerka Zipperle

  • Johannes P M Langedijk

  • Claes Orvell

  • Marc Vandevelde

  • Andreas Zurbriggen

  • Philippe Plattet

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free