Porcine reproductive and respiratory syndrome virus attachment is mediated by the N-terminal domain of the sialoadhesin receptor

• Published in: Veterinary microbiology 2010-07, Vol.143 (2), p.371-378
• Main Authors: An, Tong-Qing, Tian, Zhi-Jun, He, Yun-Xia, Xiao, Yan, Jiang, Yi-Feng, Peng, Jin-Mei, Zhou, Yan-Jun, Liu, Di, Tong, Guang-Zhi
• Format: Article
• Language: English
• Subjects: Animals; binding capacity; Binding domain; binding sites; biochemical mechanisms; Biological and medical sciences; cell adhesion; cell lines; Cells, Cultured; Core Binding Factors; Fundamental and applied biological sciences. Psychology; Gene Deletion; gene expression; genes; host-pathogen relationships; immune system; immunoglobulins; in vitro studies; infection; macrophages; Macrophages, Alveolar - physiology; Macrophages, Alveolar - virology; membrane glycoproteins; Membrane Glycoproteins - physiology; Microbiology; Miscellaneous; Models, Molecular; mutation; pathogenesis; porcine reproductive and respiratory syndrome; Porcine reproductive and respiratory syndrome virus; Porcine reproductive and respiratory syndrome virus (PRRSV); Porcine respiratory and reproductive syndrome virus; Porcine respiratory and reproductive syndrome virus - physiology; Protein Binding; Protein Conformation; pulmonary alveoli; Receptor; receptors; Receptors, Immunologic - physiology; Sialic Acid Binding Ig-like Lectin 1; sialic acids; Sialoadhesin; sialoadhesin receptor; Swine; Virology; Virus Attachment
• ISSN: 0378-1135; 1873-2542
• DOI: 10.1016/j.vetmic.2009.11.006

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.