PMID- 11932397
OWN - NLM
STAT- MEDLINE
DCOM- 20020510
LR  - 20240509
IS  - 0022-538X (Print)
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Linking)
VI  - 76
IP  - 9
DP  - 2002 May
TI  - Involvement of the matrix protein in attachment of porcine reproductive and 
      respiratory syndrome virus to a heparinlike receptor on porcine alveolar 
      macrophages.
PG  - 4312-20
AB  - The porcine reproductive and respiratory syndrome virus (PRRSV) has a very 
      restricted tropism for well-differentiated cells of the monocyte-macrophage 
      lineage, which is probably determined by specific receptors on these cells. In 
      this study, the importance of heparinlike molecules on porcine alveolar 
      macrophages (PAM) for PRRSV infection was determined. Heparin interacted with the 
      virus and reduced infection of PAM up to 92 or 88% for the American and European 
      types of PRRSV, respectively. Other glycosaminoglycans, similar to heparin, had 
      no significant effect on infection while heparinase treatment of PAM resulted in 
      a significant reduction of the infection. Analysis of infection kinetics showed 
      that PRRSV attachment to heparan sulfate occurs early in infection. A 
      heparin-sensitive binding step was observed which converted completely into a 
      heparin-resistant binding after 120 min at 4 degrees C. Using heparin-affinity 
      chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis 
      (SDS-PAGE), it was observed that the structural matrix (M) and nucleocapsid (N) 
      proteins attached to heparin. Nonreducing SDS-PAGE revealed that M bound to 
      heparin mainly as a complex with glycoprotein GP(5) and that the N protein bound 
      to heparin as a homodimer. GP(3), which was identified as a minor structural 
      protein of European types of PRRSV, did not bind to heparin. Since the N protein 
      is not exposed on the virion surface, it was concluded that the structural M 
      protein and the M-GP(5) complex contribute to PRRSV attachment on a heparinlike 
      receptor on PAM. This is the first report that identifies a PRRSV ligand for a 
      cell surface heparinlike receptor on PAM.
FAU - Delputte, P L
AU  - Delputte PL
AD  - Laboratory of Virology, Faculty of Veterinary Medicine, Ghent University, Ghent, 
      Belgium.
FAU - Vanderheijden, N
AU  - Vanderheijden N
FAU - Nauwynck, H J
AU  - Nauwynck HJ
FAU - Pensaert, M B
AU  - Pensaert MB
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Receptors, Virus)
RN  - 0 (Viral Matrix Proteins)
RN  - 0 (heparin receptor)
RN  - 9005-49-6 (Heparin)
RN  - EC 4.2.2.7 (Heparin Lyase)
SB  - IM
MH  - Animals
MH  - Glycosaminoglycans/pharmacology
MH  - Heparin/pharmacology
MH  - Heparin Lyase/pharmacology
MH  - Macrophages, Alveolar/*virology
MH  - Porcine respiratory and reproductive syndrome virus/metabolism/*pathogenicity
MH  - Receptors, Cell Surface/*metabolism
MH  - Receptors, Virus/metabolism
MH  - Swine
MH  - Viral Matrix Proteins/*metabolism
PMC - PMC155060
EDAT- 2002/04/05 10:00
MHDA- 2002/05/11 10:01
PMCR- 2002/05/01
CRDT- 2002/04/05 10:00
PHST- 2002/04/05 10:00 [pubmed]
PHST- 2002/05/11 10:01 [medline]
PHST- 2002/04/05 10:00 [entrez]
PHST- 2002/05/01 00:00 [pmc-release]
AID - 1432 [pii]
AID - 10.1128/jvi.76.9.4312-4320.2002 [doi]
PST - ppublish
SO  - J Virol. 2002 May;76(9):4312-20. doi: 10.1128/jvi.76.9.4312-4320.2002.