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效应蛋白AvrPiz-t靶向的核孔蛋白98同源物APIP12参与水稻对稻瘟病菌的基础抗性。

The Nup98 Homolog APIP12 Targeted by the Effector AvrPiz-t is Involved in Rice Basal Resistance Against Magnaporthe oryzae.

作者信息

Tang Mingzhi, Ning Yuese, Shu Xiaoli, Dong Bo, Zhang Hongyan, Wu Dianxing, Wang Hua, Wang Guo-Liang, Zhou Bo

机构信息

Institute of Nuclear-Agricultural Sciences, Zhejiang University, Hangzhou, China.

Institute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.

出版信息

Rice (N Y). 2017 Dec;10(1):5. doi: 10.1186/s12284-017-0144-7. Epub 2017 Feb 15.

DOI:10.1186/s12284-017-0144-7
PMID:28205154
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5311014/
Abstract

BACKGROUND

The effector AvrPiz-t of Magnaporthe oryzae has virulence function in rice. However, the mechanism underlying its virulence in host is not fully understood.

RESULTS

In this study, we analyzed the function of AvrPiz-t interacting protein 12 (APIP12) in rice immunity. APIP12 significantly bound to AvrPiz-t and APIP6 in its middle portion and N-terminus, respectively, in yeast two-hybrid assay. Glutathione S-transferase (GST) pull-down assay further verified the interactions of APIP12 with AvrPiz-t and APIP6. APIP12 encodes a homologue of nucleoporin protein Nup98 without the conserved domain of Phe-Gly repeats and has no orthologue in other plants. Both knockout and knockdown of APIP12 caused enhanced susceptibility of rice plants to virulent isolates of M. oryzae. The expression of some pathogenesis-related (PR) genes was reduced in both knockout and knockdown mutants, suggesting that APIP12 is required for the accumulation of transcripts of PR genes upon the infection. It is worth noting that neither knockout/knockdown nor overexpression of APIP12 attenuates Piz-t resistance.

CONCLUSIONS

Taken together, our results demonstrate that APIP12 is a virulence target of AvrPiz-t and is involved in the basal resistance against M. oryzae in rice.

摘要

背景

稻瘟病菌的效应子AvrPiz-t在水稻中具有致病功能。然而，其在宿主中致病的机制尚未完全明确。

结果

在本研究中，我们分析了AvrPiz-t互作蛋白12（APIP12）在水稻免疫中的功能。在酵母双杂交试验中，APIP12分别在其中部和N端与AvrPiz-t和APIP6显著结合。谷胱甘肽S-转移酶（GST）下拉试验进一步验证了APIP12与AvrPiz-t和APIP6之间的相互作用。APIP12编码一种核孔蛋白Nup98的同源物，没有Phe-Gly重复的保守结构域，且在其他植物中没有直系同源物。APIP12的敲除和敲低均导致水稻植株对稻瘟病菌强毒株的易感性增强。在敲除和敲低突变体中，一些病程相关（PR）基因的表达均降低，这表明APIP12是PR基因转录本在感染后积累所必需的。值得注意的是，APIP12的敲除/敲低或过表达均未减弱Piz-t抗性。

结论

综上所述，我们的结果表明APIP12是AvrPiz-t的致病靶点，并参与水稻对稻瘟病菌的基础抗性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/99cc/5311014/11b895638eac/12284_2017_144_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/99cc/5311014/8c1180115290/12284_2017_144_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/99cc/5311014/0d1dcd604558/12284_2017_144_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/99cc/5311014/c3a4490653c7/12284_2017_144_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/99cc/5311014/020ffd377e1a/12284_2017_144_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/99cc/5311014/11b895638eac/12284_2017_144_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/99cc/5311014/8c1180115290/12284_2017_144_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/99cc/5311014/0d1dcd604558/12284_2017_144_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/99cc/5311014/c3a4490653c7/12284_2017_144_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/99cc/5311014/020ffd377e1a/12284_2017_144_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/99cc/5311014/11b895638eac/12284_2017_144_Fig5_HTML.jpg

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