Structural prediction of porcine sialoadhesin V-set Ig-like domain sheds some light on its role in porcine reproductive and respiratory syndrome virus(PRRSV) infection

• Published in: Frontiers of Agricultural Science and Engineering Vol. 3; no. 1; pp. 65 - 71
• Main Authors: HOU, Jie, LI, Rui, MA, Hongfang, QIAO, Songlin, ZHANG, Gaiping
• Format: Journal Article
• Language: English
• Published: Higher Education Press 01.03.2016
• Subjects: crystallization; Drosophila S2 cell; porcine sialoadhesin; PRRSV; PRRSV|porcine sialoadhesin|V-set Ig-like domain|Drosophila S2 cell|crystallization; V-set Ig-like domain
• ISSN: 2095-7505; 2095-977X
• DOI: 10.15302/J-FASE-2016086

Porcine reproductive and respiratory syndrome(PRRS) is characterized by reproductive failures in sows and respiratory diseases in pigs of all ages. PRRS virus(PRRSV) is its causative agent and has caused huge economic losses in the swine industry. Porcine sialoadhesin(pSn) is a putative receptor of PRRSV. Previous studies have shown that a pSn V-set Ig-like domain is signi ficant in PRRSV infection. However, its structural details are not fully known, hindering our deep understanding of PRRSV infection. In this study, we successfully cloned, expressed and puri fied the p Sn V-set Ig-like domain in Drosophila S2 cells. Then we tried to crystallize the target protein and predicted its structure. This will establish the foundation for the further structural study of p Sn, deepen our understanding of the invasion mechanism of PRRSV,and support the structural information for the development of clinical drugs and vaccines against PRRSV.