The V domain of dog PVRL4 (nectin-4) mediates canine distemper virus entry and virus cell-to-cell spread
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. - 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.
- Authors:
-
- The Department of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 1X5 (Canada)
- Publication Date:
- OSTI Identifier:
- 22435027
- Resource Type:
- Journal Article
- Journal Name:
- Virology
- Additional Journal Information:
- Journal Volume: 454-455; Other Information: Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0042-6822
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 60 APPLIED LIFE SCIENCES; AMINO ACIDS; CELL MEMBRANES; DOGS; MEASLES; POLIO VIRUS; RECEPTORS; RESIDUES
Citation Formats
Delpeut, Sebastien, Noyce, Ryan S., IWK Health Centre, Canadian Center for Vaccinology, Goldbloom Pavilion, Halifax, Nova Scotia, Canada B3H 1X5, Richardson, Christopher D., E-mail: chris.richardson@dal.ca, IWK Health Centre, Canadian Center for Vaccinology, Goldbloom Pavilion, Halifax, Nova Scotia, Canada B3H 1X5, and The Department of Pediatrics, Dalhousie University, Halifax, Nova Scotia. The V domain of dog PVRL4 (nectin-4) mediates canine distemper virus entry and virus cell-to-cell spread. United States: N. p., 2014.
Web. doi:10.1016/J.VIROL.2014.02.014.
Delpeut, Sebastien, Noyce, Ryan S., IWK Health Centre, Canadian Center for Vaccinology, Goldbloom Pavilion, Halifax, Nova Scotia, Canada B3H 1X5, Richardson, Christopher D., E-mail: chris.richardson@dal.ca, IWK Health Centre, Canadian Center for Vaccinology, Goldbloom Pavilion, Halifax, Nova Scotia, Canada B3H 1X5, & The Department of Pediatrics, Dalhousie University, Halifax, Nova Scotia. The V domain of dog PVRL4 (nectin-4) mediates canine distemper virus entry and virus cell-to-cell spread. United States. https://doi.org/10.1016/J.VIROL.2014.02.014
Delpeut, Sebastien, Noyce, Ryan S., IWK Health Centre, Canadian Center for Vaccinology, Goldbloom Pavilion, Halifax, Nova Scotia, Canada B3H 1X5, Richardson, Christopher D., E-mail: chris.richardson@dal.ca, IWK Health Centre, Canadian Center for Vaccinology, Goldbloom Pavilion, Halifax, Nova Scotia, Canada B3H 1X5, and The Department of Pediatrics, Dalhousie University, Halifax, Nova Scotia. 2014.
"The V domain of dog PVRL4 (nectin-4) mediates canine distemper virus entry and virus cell-to-cell spread". United States. https://doi.org/10.1016/J.VIROL.2014.02.014.
@article{osti_22435027,
title = {The V domain of dog PVRL4 (nectin-4) mediates canine distemper virus entry and virus cell-to-cell spread},
author = {Delpeut, Sebastien and Noyce, Ryan S. and IWK Health Centre, Canadian Center for Vaccinology, Goldbloom Pavilion, Halifax, Nova Scotia, Canada B3H 1X5 and Richardson, Christopher D., E-mail: chris.richardson@dal.ca and IWK Health Centre, Canadian Center for Vaccinology, Goldbloom Pavilion, Halifax, Nova Scotia, Canada B3H 1X5 and The Department of Pediatrics, Dalhousie University, Halifax, Nova Scotia},
abstractNote = {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. - 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.},
doi = {10.1016/J.VIROL.2014.02.014},
url = {https://www.osti.gov/biblio/22435027},
journal = {Virology},
issn = {0042-6822},
number = ,
volume = 454-455,
place = {United States},
year = {Tue Apr 15 00:00:00 EDT 2014},
month = {Tue Apr 15 00:00:00 EDT 2014}
}