Division of Swine Infectious Diseases, National Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150001, China.
Vet Microbiol. 2010 Jul 14;143(2-4):371-8. doi: 10.1016/j.vetmic.2009.11.006. Epub 2009 Dec 6.
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.
唾液酸粘附素（Sn）是猪繁殖与呼吸综合征病毒（PRRSV）附着和内化到猪肺泡巨噬细胞（PAM）的重要受体。为了研究 Sn 的 N 端结构域是否足以或有必要用于 PRRSV 附着，我们构建了一系列猪 Sn 的截断片段，并在非允许性 PK15 细胞系中表达这些片段。由 Sn N 端区域的整个第一结构域组成的前 150 个氨基酸对于 PRRSV 与细胞的结合是必要的，而单独的 N 端结构域足以用于病毒附着。多克隆抗血清针对猪 Sn 的 N 端区域以剂量依赖的方式抑制 PRRSV 与 PAM 细胞的附着。本研究表明，Sn 的 N 端的第一结构域介导 PRRSV 与 PAM 细胞的附着，并有助于更好地理解 PRRSV 与其宿主细胞之间的相互作用。
