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Journal of Virology, September 2007, p. 9546-9550, Vol. 81, No. 17
0022-538X/07/$08.00+0 doi:10.1128/JVI.00569-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Wander Van Breedam,1,
Iris Delrue,1
Cornelia Oetke,2
Paul R. Crocker,2 and
Hans J. Nauwynck1
Laboratory of Virology, Department Virology, Parasitology, and Immunology, Faculty of Veterinary Medicine, Ghent University, Merelbeke, Belgium,1 Division of Cell Biology and Immunology, Wellcome Trust Biocentre, University of Dundee, Dundee, United Kingdom2
Received 19 March 2007/ Accepted 24 May 2007
The sialic acid-binding lectin sialoadhesin (Sn) is a macrophage-restricted receptor for porcine reproductive and respiratory syndrome virus (PRRSV). To investigate the importance of pSn sialic acid-binding activity for PRRSV infection, an R116-to-E mutation was introduced in the predicted sialic acid-binding domain of pSn, resulting in a mutant, pSnRE, that could not bind sialic acids. PSn, but not pSnRE, allowed PRRSV binding and internalization. These data show that the sialic acid-binding activity of pSn is essential for PRRSV attachment to pSn and thus identifies the variable, N-terminal domain of Sn as a PRRSV binding domain.
Published ahead of print on 13 June 2007.
Peter L. Delputte and Wander Van Breedam contributed equally to this work.
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