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Journal of Virology, August 2004, p. 8094-8101, Vol. 78, No. 15
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.15.8094-8101.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

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

Peter L. Delputte and Hans J. Nauwynck*

Laboratory of Virology, Department of Virology, Parasitology, and Immunology, Faculty of Veterinary Medicine, Ghent University, Ghent, Belgium

Received 30 October 2003/ Accepted 19 March 2004

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 {alpha}2-3- and {alpha}2-6-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.

* Corresponding author. Mailing address: Laboratory of Virology, Department of Virology, Parasitology, and Immunology, Faculty of Veterinary Medicine, Salisburylaan 133, 9820 Merelbeke, Belgium. Phone: 32 9 264 73 66. Fax: 32 9 264 74 95. E-mail: hans.nauwynck{at}UGent.be.

Journal of Virology, August 2004, p. 8094-8101, Vol. 78, No. 15
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.15.8094-8101.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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