Abstract
Porcine reproductive and respiratory syn- drome (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 sialoadhe- sin (pSn) is a putative receptor of PRRSV. Previous studies have shown that a pSn V-set Ig-like domain is significant in PRRSVinfection. However, its structural details are not fully known, hindering our deep understanding of PRRSV infection. In this study, we successfully cloned, expressed and purified the pSn 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 pSn, deepen our understanding of the invasion mechanism of PRRSV, and support the structural information for the development of clinical drugs and vaccines against PRRSV.
Highlights
Porcine reproductive and respiratory syndrome (PRRS) was first reported in the late 1980s in the USA
Our work provides the molecular basis for further structural study of Porcine sialoadhesin (pSn), supports its role in PRRS virus (PRRSV) infection, and may help in the elucidation of PRRSV invasion
The relative molecular mass of this band was consistent with the theoretical mass value of pSn V-set Ig-like domain with enzyme sites and His-tag, which suggests it might be the target protein
Summary
Porcine reproductive and respiratory syndrome (PRRS) was first reported in the late 1980s in the USA. It has subsequently spread worldwide, and has become endemic in countries with a high level of swine rearing[1]. PRRSV causes enormous economic losses in the swine industry every year[6] and there are many studies focusing on its infection mechanism, including its host and receptors[7]. Swine are the only known natural host of PRRSV, with myeloid cells, alveolar macrophages and dendritic cells, being the primary permissive cells. Virus invasion has been further shown to be mediated by the host cell surface receptors[8]
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