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The M/GP(5) glycoprotein complex of porcine reproductive and respiratory syndrome virus binds the sialoadhesin receptor in a sialic acid-dependent manner

Wander Van Breedam UGent, Hanne Van Gorp UGent, Jiquan Q Zhang, Paul R Crocker, Peter Delputte and Hans Nauwynck UGent (2010) PLOS PATHOGENS. 6(1).
abstract
The porcine reproductive and respiratory syndrome virus (PRRSV) is a major threat to swine health worldwide and is considered the most significant viral disease in the swine industry today. In past years, studies on the entry of the virus into its host cell have led to the identification of a number of essential virus receptors and entry mediators. However, viral counterparts for these molecules have remained elusive and this has made rational development of new generation vaccines impossible. The main objective of this study was to identify the viral counterparts for sialoadhesin, a crucial PRRSV receptor on macrophages. For this purpose, a soluble form of sialoadhesin was constructed and validated. The soluble sialoadhesin could bind PRRSV in a sialic acid-dependent manner and could neutralize PRRSV infection of macrophages, thereby confirming the role of sialoadhesin as an essential PRRSV receptor on macrophages. Although sialic acids are present on the GP(3), GP(4) and GP(5) envelope glycoproteins, only the M/GP(5) glycoprotein complex of PRRSV was identified as a ligand for sialoadhesin. The interaction was found to be dependent on the sialic acid binding capacity of sialoadhesin and on the presence of sialic acids on GP(5). These findings not only contribute to a better understanding of PRRSV biology, but the knowledge and tools generated in this study also hold the key to the development of a new generation of PRRSV vaccines.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
IMMUNOGLOBULIN SUPERFAMILY, IMMUNE-SYSTEM, NEUTRALIZATION EPITOPE, STRUCTURAL PROTEINS, LELYSTAD-VIRUS, MONOCLONAL-ANTIBODIES, ALVEOLAR MACROPHAGES, SYNDROME PRRS VIRUS, MYSTERY SWINE DISEASE, ISOLATE ATCC VR-2332
journal title
PLOS PATHOGENS
PLoS Pathog.
volume
6
issue
1
pages
11 pages
Web of Science type
Article
Web of Science id
000274227100021
JCR category
VIROLOGY
JCR impact factor
9.079 (2010)
JCR rank
1/32 (2010)
JCR quartile
1 (2010)
ISSN
1553-7366
DOI
10.1371/journal.ppat.1000730
language
English
UGent publication?
yes
classification
A1
additional info
article no. e1000730 (11 p.)
copyright statement
I have retained and own the full copyright for this publication
id
873669
handle
http://hdl.handle.net/1854/LU-873669
date created
2010-02-22 15:07:07
date last changed
2016-12-19 15:39:30
@article{873669,
  abstract     = {The porcine reproductive and respiratory syndrome virus (PRRSV) is a major threat to swine health worldwide and is considered the most significant viral disease in the swine industry today. In past years, studies on the entry of the virus into its host cell have led to the identification of a number of essential virus receptors and entry mediators. However, viral counterparts for these molecules have remained elusive and this has made rational development of new generation vaccines impossible. The main objective of this study was to identify the viral counterparts for sialoadhesin, a crucial PRRSV receptor on macrophages. For this purpose, a soluble form of sialoadhesin was constructed and validated. The soluble sialoadhesin could bind PRRSV in a sialic acid-dependent manner and could neutralize PRRSV infection of macrophages, thereby confirming the role of sialoadhesin as an essential PRRSV receptor on macrophages. Although sialic acids are present on the GP(3), GP(4) and GP(5) envelope glycoproteins, only the M/GP(5) glycoprotein complex of PRRSV was identified as a ligand for sialoadhesin. The interaction was found to be dependent on the sialic acid binding capacity of sialoadhesin and on the presence of sialic acids on GP(5). These findings not only contribute to a better understanding of PRRSV biology, but the knowledge and tools generated in this study also hold the key to the development of a new generation of PRRSV vaccines.},
  author       = {Van Breedam, Wander and Van Gorp, Hanne and Zhang, Jiquan Q and Crocker, Paul R and Delputte, Peter and Nauwynck, Hans},
  issn         = {1553-7366},
  journal      = {PLOS PATHOGENS},
  keyword      = {IMMUNOGLOBULIN SUPERFAMILY,IMMUNE-SYSTEM,NEUTRALIZATION EPITOPE,STRUCTURAL PROTEINS,LELYSTAD-VIRUS,MONOCLONAL-ANTIBODIES,ALVEOLAR MACROPHAGES,SYNDROME PRRS VIRUS,MYSTERY SWINE DISEASE,ISOLATE ATCC VR-2332},
  language     = {eng},
  number       = {1},
  pages        = {11},
  title        = {The M/GP(5) glycoprotein complex of porcine reproductive and respiratory syndrome virus binds the sialoadhesin receptor in a sialic acid-dependent manner},
  url          = {http://dx.doi.org/10.1371/journal.ppat.1000730},
  volume       = {6},
  year         = {2010},
}

Chicago
Van Breedam, Wander, Hanne Van Gorp, Jiquan Q Zhang, Paul R Crocker, Peter Delputte, and Hans Nauwynck. 2010. “The M/GP(5) Glycoprotein Complex of Porcine Reproductive and Respiratory Syndrome Virus Binds the Sialoadhesin Receptor in a Sialic Acid-dependent Manner.” Plos Pathogens 6 (1).
APA
Van Breedam, W., Van Gorp, H., Zhang, J. Q., Crocker, P. R., Delputte, P., & Nauwynck, H. (2010). The M/GP(5) glycoprotein complex of porcine reproductive and respiratory syndrome virus binds the sialoadhesin receptor in a sialic acid-dependent manner. PLOS PATHOGENS, 6(1).
Vancouver
1.
Van Breedam W, Van Gorp H, Zhang JQ, Crocker PR, Delputte P, Nauwynck H. The M/GP(5) glycoprotein complex of porcine reproductive and respiratory syndrome virus binds the sialoadhesin receptor in a sialic acid-dependent manner. PLOS PATHOGENS. 2010;6(1).
MLA
Van Breedam, Wander, Hanne Van Gorp, Jiquan Q Zhang, et al. “The M/GP(5) Glycoprotein Complex of Porcine Reproductive and Respiratory Syndrome Virus Binds the Sialoadhesin Receptor in a Sialic Acid-dependent Manner.” PLOS PATHOGENS 6.1 (2010): n. pag. Print.