Molecular characterization of limulin, a sialic acid binding lectin from the hemolymph of the horseshoe crab, Limulus polyphemus

Biochemistry ◽  
1977 ◽  
Vol 16 (19) ◽  
pp. 4297-4303 ◽  
Author(s):  
Ruth Kaplan ◽  
Steven S. L. Li ◽  
J. Michael Kehoe
Keyword(s):  
Sialic Acid ◽  
Molecular Characterization ◽  
Horseshoe Crab ◽  
Limulus Polyphemus ◽  
Sialic Acid Binding ◽  
Binding Lectin

Further characterization of the sialic acid-binding lectin from the horseshoe crab Carcinoscorpius rotunda cauda

1981 ◽  
Vol 209 (1) ◽  
pp. 325-333 ◽  
Author(s):  
D.Thambi Dorai ◽  
B.K. Bachhawat ◽  
S. Bishayee ◽  
K. Kannan ◽  
D.Rajagopal Rao
Keyword(s):  
Sialic Acid ◽  
Horseshoe Crab ◽  
Sialic Acid Binding ◽  
Binding Lectin

scholarly journals On the multispecificity of carcinoscorpin, the sialic acid binding lectin from the horseshoe crab Carcinoscorpius rotundacauda

FEBS Letters ◽  
1982 ◽  
Vol 148 (1) ◽  
pp. 98-102 ◽  
Author(s):  
Devarajan Thambi Dorai ◽  
Mohan Somasundaran ◽  
Subita Srimal ◽  
Bimal Kumar Bachhawat
Keyword(s):  
Sialic Acid ◽  
Horseshoe Crab ◽  
Sialic Acid Binding ◽  
Binding Lectin

scholarly journals Porcine Arterivirus Infection of Alveolar Macrophages Is Mediated by Sialic Acid on the Virus

2004 ◽  
Vol 78 (15) ◽  
pp. 8094-8101 ◽  
Author(s):  
Peter L. Delputte ◽  
Hans J. Nauwynck
Keyword(s):  
Sialic Acid ◽  
Alveolar Macrophages ◽  
Sialic Acids ◽  
Respiratory Syndrome Virus ◽  
Specific Monoclonal Antibody ◽  
Neuraminidase Treatment ◽  
Acid Binding Protein ◽  
Sialic Acid Binding ◽  
High Mannose ◽  
Binding Lectin

ABSTRACT 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 α2-3- and α2-6-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.

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