title: Porcine reproductive and respiratory syndrome virus attachment is mediated by the N-terminal domain of the sialoadhesin receptor.
abstract: Sialoadhesin (Sn) is an important receptor for viral attachment and internalization of porcine reproductive and respiratory syndrome virus (PRRSV) to porcine alveolar macrophages (PAM). To investigate whether the N-terminal domain of Sn is sufficient and/or necessary for PRRSV attachment, we constructed a series of truncated fragments of porcine Sn and expressed these in the non-permissive PK15 cell line. The first 150 amino acids comprising the entire first domain of the Sn N-terminal region was necessary for PRRSV binding to cells, and the N-terminal domain alone was sufficient for virus attachment. The attachment of PRRSV to PAM cells was inhibited by polyclonal anti-serum against the N-terminal region of porcine Sn in a dose-dependent manner. The present study demonstrates that the first domain at the N-terminus of Sn mediates PRRSV attachment to PAM cells and contributes to better understanding the interaction between PRRSV and its host cells.
authors.affiliation: Division of Swine Infectious Diseases, National Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150001, China.
authors.forename: Tong-Qing
authors.initials: TQ
authors.lastname: An
authors.forename: Zhi-Jun
authors.initials: ZJ
authors.lastname: Tian
authors.forename: Yun-Xia
authors.initials: YX
authors.lastname: He
authors.forename: Yan
authors.initials: Y
authors.lastname: Xiao
authors.forename: Yi-Feng
authors.initials: YF
authors.lastname: Jiang
authors.forename: Jin-Mei
authors.initials: JM
authors.lastname: Peng
authors.forename: Yan-Jun
authors.initials: YJ
authors.lastname: Zhou
authors.forename: Di
authors.initials: D
authors.lastname: Liu
authors.forename: Guang-Zhi
authors.initials: GZ
authors.lastname: Tong
mesh_terms: D000818:Animals; D002478:Cells, Cultured; D050660:Core Binding Factors; D017353:Gene Deletion; D016676:Macrophages, Alveolar / Q000502:physiology / Q000821:virology*; D008562:Membrane Glycoproteins / Q000502:physiology*; D008958:Models, Molecular; D019316:Porcine respiratory and reproductive syndrome virus / Q000502:physiology*; D011485:Protein Binding; D011487:Protein Conformation; D011971:Receptors, Immunologic / Q000502:physiology*; D063267:Sialic Acid Binding Ig-like Lectin 1; D013552:Swine; D053585:Virus Attachment
chemical_list: D050660:Core Binding Factors; D008562:Membrane Glycoproteins; D011971:Receptors, Immunologic; D063267:Sialic Acid Binding Ig-like Lectin 1