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Title: Canine and feline parvoviruses preferentially recognize the non-human cell surface sialic acid N-glycolylneuraminic acid

Abstract

Feline panleukopenia virus (FPV) is a pathogen whose canine-adapted form (canine parvovirus (CPV)) emerged in 1978. These viruses infect by binding host transferrin receptor type-1 (TfR), but also hemagglutinate erythrocytes. We show that hemagglutination involves selective recognition of the non-human sialic acid N-glycolylneuraminic acid (Neu5Gc) but not N-acetylneuraminic acid (Neu5Ac), which differs by only one oxygen atom from Neu5Gc. Overexpression of α2-6 sialyltransferase did not change binding, indicating that both α2-3 and α2-6 linkages are recognized. However, Neu5Gc expression on target cells did not enhance CPV or FPV infection in vitro. Thus, the conserved Neu5Gc-binding preference of these viruses likely plays a role in the natural history of the virus in vivo. Further studies must clarify relationships between virus infection and host Neu5Gc expression. As a first step, we show that transcripts of CMAH (which generates Neu5Gc from Neu5Ac) are at very low levels in Western dog breed cells. - Highlights: ► Feline and canine parvoviruses recognize Neu5Gc but not Neu5Ac, which differ by one oxygen atom. ► The underlying linkage of these sialic acids does not affect recognition. ► Induced Neu5Gc expression on target cells that normally express Neu5Ac did not enhance infection. ► Thus, the conserved binding preferencemore » plays an important yet unknown role in in vivo infections. ► Population and breed variations in Neu5Gc expression occur, likely by regulating the gene CMAH.« less

Authors:
 [1]; ;  [2];  [1]
  1. Departments of Medicine and Cellular and Molecular Medicine, Glycobiology Research and Training Center, Center for Academic Research and Training in Anthropogeny, 9500 Gilman Drive, University of California, San Diego, La Jolla, CA 92093 (United States)
  2. Baker Institute for Animal Health, Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853 (United States)
Publication Date:
OSTI Identifier:
22423732
Resource Type:
Journal Article
Journal Name:
Virology
Additional Journal Information:
Journal Volume: 440; Journal Issue: 1; Other Information: Copyright (c) 2013 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; DOGS; ERYTHROCYTES; GENES; HEMAGGLUTININS; IN VITRO; IN VIVO; OXYGEN; PATHOGENS; RECEPTORS; SIALIC ACID; SURFACES; TRANSFERRIN; VIRUSES

Citation Formats

Löfling, Jonas, Michael Lyi, Sangbom, Parrish, Colin R., and Varki, Ajit. Canine and feline parvoviruses preferentially recognize the non-human cell surface sialic acid N-glycolylneuraminic acid. United States: N. p., 2013. Web. doi:10.1016/J.VIROL.2013.02.009.
Löfling, Jonas, Michael Lyi, Sangbom, Parrish, Colin R., & Varki, Ajit. Canine and feline parvoviruses preferentially recognize the non-human cell surface sialic acid N-glycolylneuraminic acid. United States. https://doi.org/10.1016/J.VIROL.2013.02.009
Löfling, Jonas, Michael Lyi, Sangbom, Parrish, Colin R., and Varki, Ajit. 2013. "Canine and feline parvoviruses preferentially recognize the non-human cell surface sialic acid N-glycolylneuraminic acid". United States. https://doi.org/10.1016/J.VIROL.2013.02.009.
@article{osti_22423732,
title = {Canine and feline parvoviruses preferentially recognize the non-human cell surface sialic acid N-glycolylneuraminic acid},
author = {Löfling, Jonas and Michael Lyi, Sangbom and Parrish, Colin R. and Varki, Ajit},
abstractNote = {Feline panleukopenia virus (FPV) is a pathogen whose canine-adapted form (canine parvovirus (CPV)) emerged in 1978. These viruses infect by binding host transferrin receptor type-1 (TfR), but also hemagglutinate erythrocytes. We show that hemagglutination involves selective recognition of the non-human sialic acid N-glycolylneuraminic acid (Neu5Gc) but not N-acetylneuraminic acid (Neu5Ac), which differs by only one oxygen atom from Neu5Gc. Overexpression of α2-6 sialyltransferase did not change binding, indicating that both α2-3 and α2-6 linkages are recognized. However, Neu5Gc expression on target cells did not enhance CPV or FPV infection in vitro. Thus, the conserved Neu5Gc-binding preference of these viruses likely plays a role in the natural history of the virus in vivo. Further studies must clarify relationships between virus infection and host Neu5Gc expression. As a first step, we show that transcripts of CMAH (which generates Neu5Gc from Neu5Ac) are at very low levels in Western dog breed cells. - Highlights: ► Feline and canine parvoviruses recognize Neu5Gc but not Neu5Ac, which differ by one oxygen atom. ► The underlying linkage of these sialic acids does not affect recognition. ► Induced Neu5Gc expression on target cells that normally express Neu5Ac did not enhance infection. ► Thus, the conserved binding preference plays an important yet unknown role in in vivo infections. ► Population and breed variations in Neu5Gc expression occur, likely by regulating the gene CMAH.},
doi = {10.1016/J.VIROL.2013.02.009},
url = {https://www.osti.gov/biblio/22423732}, journal = {Virology},
issn = {0042-6822},
number = 1,
volume = 440,
place = {United States},
year = {Sat May 25 00:00:00 EDT 2013},
month = {Sat May 25 00:00:00 EDT 2013}
}