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

Abstract

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 significant 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 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.

Keywords

PRRSV / porcine sialoadhesin / V-set Ig-like domain / Drosophila S2 cell / crystallization

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Acknowledgements

This study was supported by the National Natural Science Foundation of China (31490601), the National Program on the Key Basic Research Project (2014CB542702), and the Basic and Advanced Technology Research Program of Henan Province (162300410252). The Drosophila Expression System was kindly provided by Professor Mingdong Huang (Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, China).

Jie Hou, Rui Li, Hongfang Ma, Songlin Qiao, and Gaiping Zhang declare that they have no conflict of interest or financial conflicts to disclose.

This article does not contain any studies with human or animal subjects performed by any of the authors.

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Higher Education Press and Springer-Verlag Berlin Heidelberg