HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Delputte, P. L. Articles by Nauwynck, H. J. Search for Related Content PubMed PubMed Citation Articles by Delputte, P. L. Articles by Nauwynck, H. J. Agricola Articles by Delputte, P. L. Articles by Nauwynck, H. J.

Analysis of porcine reproductive and respiratory syndrome virus attachment and internalization: distinctive roles for heparan sulphate and sialoadhesin

Laboratory of Virology, Department of Virology, Parasitology and Immunology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, 9820 Merelbeke, Belgium

Correspondence
H. J. Nauwynck
hans.nauwynck{at}UGent.be

Heparan sulphate and sialoadhesin were previously identified on porcine macrophages as receptors for porcine reproductive and respiratory syndrome virus (PRRSV). In this study, the exact role and cooperation of heparan sulphate and sialoadhesin during PRRSV attachment and internalization was analysed. It was observed that both heparan sulphate and sialoadhesin mediate PRRSV attachment and that only these two receptors are involved in attachment. Analysis of attachment kinetics of PRRSV to macrophages revealed that early attachment is mediated mainly via an interaction with heparan sulphate, followed by a gradual increase in interaction with sialoadhesin. By using wild-type CHO and CHO deficient in heparan sulphate expression, it was shown that heparan sulphate alone is sufficient to mediate PRRSV attachment, but not entry, and that heparan sulphate is not necessary for sialoadhesin to function as a PRRSV internalization receptor, but enhances the interaction of the virus with sialoadhesin.

This article has been cited by other articles:

				H. Van Gorp, W. Van Breedam, P. L. Delputte, and H. J. Nauwynck Sialoadhesin and CD163 join forces during entry of the porcine reproductive and respiratory syndrome virus J. Gen. Virol., December 1, 2008; 89(12): 2943 - 2953. [Abstract] [Full Text] [PDF]

				P. L. Delputte, W. Van Breedam, I. Delrue, C. Oetke, P. R. Crocker, and H. J. Nauwynck Porcine Arterivirus Attachment to the Macrophage-Specific Receptor Sialoadhesin Is Dependent on the Sialic Acid-Binding Activity of the N-Terminal Immunoglobulin Domain of Sialoadhesin J. Virol., September 1, 2007; 81(17): 9546 - 9550. [Abstract] [Full Text] [PDF]

				J. G. Calvert, D. E. Slade, S. L. Shields, R. Jolie, R. M. Mannan, R. G. Ankenbauer, and S.-K. W. Welch CD163 Expression Confers Susceptibility to Porcine Reproductive and Respiratory Syndrome Viruses J. Virol., July 15, 2007; 81(14): 7371 - 7379. [Abstract] [Full Text] [PDF]

				S. Costers, P. L. Delputte, and H. J. Nauwynck Porcine reproductive and respiratory syndrome virus-infected alveolar macrophages contain no detectable levels of viral proteins in their plasma membrane and are protected against antibody-dependent, complement-mediated cell lysis. J. Gen. Virol., August 1, 2006; 87(Pt 8): 2341 - 2351. [Abstract] [Full Text] [PDF]

				G. Misinzo, P. L. Delputte, P. Meerts, D. J. Lefebvre, and H. J. Nauwynck Porcine circovirus 2 uses heparan sulfate and chondroitin sulfate B glycosaminoglycans as receptors for its attachment to host cells. J. Virol., April 1, 2006; 80(7): 3487 - 3494. [Abstract] [Full Text] [PDF]