☆ 4.5 Article

Amino acid at position 176 was essential for porcine reproductive and respiratory syndrome virus (PRRSV) non-structural protein 1α (nsp1α) as an inhibitor to the induction of IFN-β

CELLULAR IMMUNOLOGY (2012)

期刊

CELLULAR IMMUNOLOGY

卷 280, 期 2, 页码 125-131

出版社

ACADEMIC PRESS INC ELSEVIER SCIENCE

DOI: 10.1016/j.cellimm.2012.10.003

关键词

Porcine reproductive and respiratory syndrome virus (PRRSV); Nonstructural protein 1 alpha; Interferon-beta

类别

Cell Biology Immunology

资金

Key Program National Natural Science Foundation of China [30730068, 31072122]

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摘要

Previous studies have shown that porcine reproductive and respiratory syndrome virus (PRRSV) non-structural protein 1 alpha (nsp1 alpha) was the interferon (IFN) antagonist. However, the mechanism was unclear. In the present study, deletion of the carboxyl-terminal extension (CTE) (167-180 amino acid (aa)) made nsp1 alpha lose its inhibitory ability to the induction of IFN-beta. And a series of C-terminal truncated mutants for nsp1 alpha showed that 1-176 aa of nsp1 alpha was able to inhibit the induction of IFN-beta and deleting or mutating the amino acid F176 made nsp1 alpha not inhibit the induction of IFN-beta. In conclusion, the CTE and the amino acid F176 were critical for nsp1 alpha as the IFN antagonist and the region representing 167-176 was the minimal subunit of the CTE for nsp1 alpha to retain its suppressive activity to the induction of IFN-beta. (C) 2012 Published by Elsevier Inc.

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