PMID- 20084110
OWN - NLM
STAT- MEDLINE
DCOM- 20100309
LR  - 20211028
IS  - 1553-7374 (Electronic)
IS  - 1553-7366 (Print)
IS  - 1553-7366 (Linking)
VI  - 6
IP  - 1
DP  - 2010 Jan 15
TI  - The M/GP(5) glycoprotein complex of porcine reproductive and respiratory syndrome 
      virus binds the sialoadhesin receptor in a sialic acid-dependent manner.
PG  - e1000730
LID - 10.1371/journal.ppat.1000730 [doi]
LID - e1000730
AB  - 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.
FAU - Van Breedam, Wander
AU  - Van Breedam W
AD  - Laboratory of Virology, Department of Virology, Parasitology and Immunology, 
      Faculty of Veterinary Medicine, Ghent University, Merelbeke, Belgium. 
      wander.vanbreedam@UGent.be
FAU - Van Gorp, Hanne
AU  - Van Gorp H
FAU - Zhang, Jiquan Q
AU  - Zhang JQ
FAU - Crocker, Paul R
AU  - Crocker PR
FAU - Delputte, Peter L
AU  - Delputte PL
FAU - Nauwynck, Hans J
AU  - Nauwynck HJ
LA  - eng
GR  - 081882/WT_/Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20100115
PL  - United States
TA  - PLoS Pathog
JT  - PLoS pathogens
JID - 101238921
RN  - 0 (Glycoproteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Sialic Acid Binding Ig-like Lectin 1)
RN  - 0 (Viral Envelope Proteins)
RN  - 0 (glycoprotein 5, PRRSV)
RN  - 0 (protein M (glycoprotein))
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Animals
MH  - Blotting, Western
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Glycoproteins/*metabolism
MH  - Macrophages/metabolism/virology
MH  - Membrane Glycoproteins/*metabolism
MH  - N-Acetylneuraminic Acid/*metabolism
MH  - Polymerase Chain Reaction
MH  - Porcine respiratory and reproductive syndrome virus/metabolism/*pathogenicity
MH  - Receptors, Immunologic/*metabolism
MH  - Recombinant Fusion Proteins/metabolism
MH  - Sialic Acid Binding Ig-like Lectin 1
MH  - Swine
MH  - Viral Envelope Proteins/*metabolism
MH  - Virus Attachment
PMC - PMC2799551
COIS- The authors have declared that no competing interests exist.
EDAT- 2010/01/20 06:00
MHDA- 2010/03/10 06:00
PMCR- 2010/01/15
CRDT- 2010/01/20 06:00
PHST- 2009/05/12 00:00 [received]
PHST- 2009/12/16 00:00 [accepted]
PHST- 2010/01/20 06:00 [entrez]
PHST- 2010/01/20 06:00 [pubmed]
PHST- 2010/03/10 06:00 [medline]
PHST- 2010/01/15 00:00 [pmc-release]
AID - 09-PLPA-RA-0770R2 [pii]
AID - 10.1371/journal.ppat.1000730 [doi]
PST - epublish
SO  - PLoS Pathog. 2010 Jan 15;6(1):e1000730. doi: 10.1371/journal.ppat.1000730.