Elsevier

Virology

Volumes 454–455, April 2014, Pages 109-117
Virology

The V domain of dog PVRL4 (nectin-4) mediates canine distemper virus entry and virus cell-to-cell spread

https://doi.org/10.1016/j.virol.2014.02.014Get rights and content
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Highlights

  • PVRL4 (nectin-4) is the epithelial cell receptor for measles and canine distemper viruses.

  • V domain of PVRL4 is critical for CDV entry, cell-to-cell spread, and syncytia formation.

  • Chimeric PVRL1 backbone substituted with the V domain of PVRL4 can function as a receptor.

  • Amino acids (F132/P133/A134/G135) within the V domain are essential for PVRL4 receptor activity.

  • Amino acids (P493/Y539) within CDV H protein are essential for PVRL4 receptor interaction.

Abstract

The entry of canine distemper virus (CDV) is a multistep process that involves the attachment of CDV hemagglutinin (H) to its cellular receptor, followed by fusion between virus and cell membranes. Our laboratory recently identified PVRL4 (nectin-4) to be the epithelial receptor for measles and canine distemper viruses. In this study, we demonstrate that the V domain of PVRL4 is critical for CDV entry and virus cell-to-cell spread. Furthermore, four key amino acid residues within the V domain of dog PVRL4 and two within the CDV hemagglutinin were shown to be essential for receptor-mediated virus entry.

Keywords

Nectin-4
PVRL4
Poliovirus receptor-like protein-4
Receptor
V domain
Epithelial cell
Canine distemper virus
CDV
Hemagglutinin
Virus entry
Syncytia formation

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1

These authors contributed equally to this work.