PMID- 15254181
OWN - NLM
STAT- MEDLINE
DCOM- 20040806
LR  - 20181113
IS  - 0022-538X (Print)
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Linking)
VI  - 78
IP  - 15
DP  - 2004 Aug
TI  - Porcine arterivirus infection of alveolar macrophages is mediated by sialic acid 
      on the virus.
PG  - 8094-101
AB  - Recently, we showed that porcine sialoadhesin (pSn) mediates internalization of 
      the arterivirus porcine reproductive and respiratory syndrome virus (PRRSV) in 
      alveolar macrophages (Vanderheijden et al., J. Virol. 77:8207-8215, 2003). In 
      rodents and humans, sialoadhesin, or Siglec-1, has been described as a 
      macrophage-restricted molecule and to specifically bind sialic acid moieties. In 
      the current study, we investigated whether pSn is a sialic acid binding protein 
      and, whether so, whether this property is important for its function as a PRRSV 
      receptor. Using untreated and neuraminidase-treated sheep erythrocytes, we showed 
      that pSn binds sialic acid. Furthermore, pSn-specific monoclonal antibody 41D3, 
      which blocks PRRSV infection, inhibited this interaction. PRRSV attachment to and 
      infection of porcine alveolar macrophages (PAM) were both shown to be dependent 
      on the presence of sialic acid on the virus: neuraminidase treatment of virus but 
      not of PAM blocked infection and reduced attachment. Enzymatic removal of all 
      N-linked glycans on the virus with N-glycosidase F reduced PRRSV infection, while 
      exclusive removal of nonsialylated N-linked glycans of the high-mannose type with 
      endoglycosidase H had no significant effect. Free sialyllactose and sialic acid 
      containing (neo)glycoproteins reduced infection, while lactose and 
      (neo)glycoproteins devoid of sialic acids had no significant effect. Studies with 
      linkage-specific neuraminidases and lectins indicated that alpha2-3- and 
      alpha2-6-linked sialic acids on the virion are important for PRRSV infection of 
      PAM. From these results, we conclude that pSn is a sialic acid binding lectin and 
      that interactions between sialic acid on the PRRS virion and pSn are essential 
      for PRRSV infection of PAM.
FAU - Delputte, Peter L
AU  - Delputte PL
AD  - Department of Virology, Faculty of Veterinary Medicine, Belgium.
FAU - Nauwynck, Hans J
AU  - Nauwynck HJ
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 (Lectins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (SIGLEC1 protein, human)
RN  - 0 (Sialic Acid Binding Ig-like Lectin 1)
RN  - EC 3.2.1.18 (Neuraminidase)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Animals
MH  - Lectins/pharmacology
MH  - Macrophages, Alveolar/*virology
MH  - Membrane Glycoproteins/physiology
MH  - N-Acetylneuraminic Acid/*physiology
MH  - Neuraminidase/pharmacology
MH  - Porcine respiratory and reproductive syndrome virus/*physiology
MH  - Receptors, Immunologic/physiology
MH  - Sheep
MH  - Sialic Acid Binding Ig-like Lectin 1
PMC - PMC446125
EDAT- 2004/07/16 05:00
MHDA- 2004/08/07 05:00
PMCR- 2004/08/01
CRDT- 2004/07/16 05:00
PHST- 2004/07/16 05:00 [pubmed]
PHST- 2004/08/07 05:00 [medline]
PHST- 2004/07/16 05:00 [entrez]
PHST- 2004/08/01 00:00 [pmc-release]
AID - 78/15/8094 [pii]
AID - 2282-03 [pii]
AID - 10.1128/JVI.78.15.8094-8101.2004 [doi]
PST - ppublish
SO  - J Virol. 2004 Aug;78(15):8094-101. doi: 10.1128/JVI.78.15.8094-8101.2004.