Open AccessPorcine 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(s) -
Peter Delputte,
Wander Van Breedam,
Iris Delrue,
Cornelia Oetke,
Paul R. Crocker,
Hans Nauwynck
Publication year - 2007
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.00569-07
Subject(s) - sialic acid , biology , porcine reproductive and respiratory syndrome virus , internalization , arterivirus , n acetylneuraminic acid , receptor , siglec , antibody , mutant , biochemistry , microbiology and biotechnology , virology , virus , immunology , gene , covid-19 , medicine , disease , pathology , infectious disease (medical specialty)
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.