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J Virol. 2007 Sep;81(17):9546-50. Epub 2007 Jun 13.

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.

Author information

  • 1Laboratory of Virology, Department Virology, Parasitology, and Immunology, Ghent University, Salisburylaan 133, B-9820 Merelbeke, Belgium. peter.delputte@UGent.be

Abstract

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 R(116)-to-E mutation was introduced in the predicted sialic acid-binding domain of pSn, resulting in a mutant, pSn(RE), that could not bind sialic acids. PSn, but not pSn(RE), 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.

PMID:
17567703
[PubMed - indexed for MEDLINE]
PMCID:
PMC1951444
Free PMC Article

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