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Role of lysine residues of the Magnaporthe oryzae effector AvrPiz-t in effector- and PAMP-triggered immunity.
Mol Plant Pathol. 2019 04; 20(4):599-608.MP

Abstract

Magnaporthe oryzae is an important fungal pathogen of both rice and wheat. However, how M. oryzae effectors modulate plant immunity is not fully understood. Previous studies have shown that the M. oryzae effector AvrPiz-t targets the host ubiquitin-proteasome system to manipulate plant defence. In return, two rice ubiquitin E3 ligases, APIP6 and APIP10, ubiquitinate AvrPiz-t for degradation. To determine how lysine residues contribute to the stability and function of AvrPiz-t, we generated double (K1,2R-AvrPiz-t), triple (K1,2,3R-AvrPiz-t) and lysine-free (LF-AvrPiz-t) mutants by mutating lysines into arginines in AvrPiz-t. LF-AvrPiz-t showed the highest protein accumulation when transiently expressed in rice protoplasts. When co-expressed with APIP10 in Nicotiana benthamiana, LF-AvrPiz-t was more stable than AvrPiz-t and was less able to degrade APIP10. The avirulence of LF-AvrPiz-t on Piz-t:HA plants was less than that of AvrPiz-t, which led to resistance reduction and lower accumulation of the Piz-t:HA protein after inoculation with the LF-AvrPiz-t-carrying isolate. Chitin- and flg22-induced production of reactive oxygen species (ROS) was higher in LF-AvrPiz-t than in AvrPiz-t transgenic plants. In addition, LF-AvrPiz-t transgenic plants were less susceptible than AvrPiz-t transgenic plants to a virulent isolate. Furthermore, both AvrPiz-t and LF-AvrPiz-t interacted with OsRac1, but the suppression of OsRac1-mediated ROS generation by LF-AvrPiz-t was significantly lower than that by AvrPiz-t. Together, these results suggest that the lysine residues of AvrPiz-t are required for its avirulence and virulence functions in rice.

Authors+Show Affiliations

Department of Plant Pathology, Ohio State University, Columbus, OH, 43210.Department of Plant Pathology, Ohio State University, Columbus, OH, 43210.Department of Plant Pathology, Ohio State University, Columbus, OH, 43210.Department of Plant Pathology, Ohio State University, Columbus, OH, 43210.Department of Plant Pathology, Ohio State University, Columbus, OH, 43210.Department of Plant Pathology, Ohio State University, Columbus, OH, 43210. State Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, 100193, China.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

30548752

Citation

Bai, Pengfei, et al. "Role of Lysine Residues of the Magnaporthe Oryzae Effector AvrPiz-t in Effector- and PAMP-triggered Immunity." Molecular Plant Pathology, vol. 20, no. 4, 2019, pp. 599-608.
Bai P, Park CH, Shirsekar G, et al. Role of lysine residues of the Magnaporthe oryzae effector AvrPiz-t in effector- and PAMP-triggered immunity. Mol Plant Pathol. 2019;20(4):599-608.
Bai, P., Park, C. H., Shirsekar, G., Songkumarn, P., Bellizzi, M., & Wang, G. L. (2019). Role of lysine residues of the Magnaporthe oryzae effector AvrPiz-t in effector- and PAMP-triggered immunity. Molecular Plant Pathology, 20(4), 599-608. https://doi.org/10.1111/mpp.12779
Bai P, et al. Role of Lysine Residues of the Magnaporthe Oryzae Effector AvrPiz-t in Effector- and PAMP-triggered Immunity. Mol Plant Pathol. 2019;20(4):599-608. PubMed PMID: 30548752.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Role of lysine residues of the Magnaporthe oryzae effector AvrPiz-t in effector- and PAMP-triggered immunity. AU - Bai,Pengfei, AU - Park,Chan-Ho, AU - Shirsekar,Gautam, AU - Songkumarn,Pattavipha, AU - Bellizzi,Maria, AU - Wang,Guo-Liang, Y1 - 2019/02/08/ PY - 2018/12/15/pubmed PY - 2020/3/31/medline PY - 2018/12/15/entrez KW - effector KW - lysine residue KW - protein stability KW - reactive oxygen species KW - rice immunity SP - 599 EP - 608 JF - Molecular plant pathology JO - Mol Plant Pathol VL - 20 IS - 4 N2 - Magnaporthe oryzae is an important fungal pathogen of both rice and wheat. However, how M. oryzae effectors modulate plant immunity is not fully understood. Previous studies have shown that the M. oryzae effector AvrPiz-t targets the host ubiquitin-proteasome system to manipulate plant defence. In return, two rice ubiquitin E3 ligases, APIP6 and APIP10, ubiquitinate AvrPiz-t for degradation. To determine how lysine residues contribute to the stability and function of AvrPiz-t, we generated double (K1,2R-AvrPiz-t), triple (K1,2,3R-AvrPiz-t) and lysine-free (LF-AvrPiz-t) mutants by mutating lysines into arginines in AvrPiz-t. LF-AvrPiz-t showed the highest protein accumulation when transiently expressed in rice protoplasts. When co-expressed with APIP10 in Nicotiana benthamiana, LF-AvrPiz-t was more stable than AvrPiz-t and was less able to degrade APIP10. The avirulence of LF-AvrPiz-t on Piz-t:HA plants was less than that of AvrPiz-t, which led to resistance reduction and lower accumulation of the Piz-t:HA protein after inoculation with the LF-AvrPiz-t-carrying isolate. Chitin- and flg22-induced production of reactive oxygen species (ROS) was higher in LF-AvrPiz-t than in AvrPiz-t transgenic plants. In addition, LF-AvrPiz-t transgenic plants were less susceptible than AvrPiz-t transgenic plants to a virulent isolate. Furthermore, both AvrPiz-t and LF-AvrPiz-t interacted with OsRac1, but the suppression of OsRac1-mediated ROS generation by LF-AvrPiz-t was significantly lower than that by AvrPiz-t. Together, these results suggest that the lysine residues of AvrPiz-t are required for its avirulence and virulence functions in rice. SN - 1364-3703 UR - https://www.unboundmedicine.com/medline/citation/30548752/Role_of_lysine_residues_of_the_Magnaporthe_oryzae_effector_AvrPiz_t_in_effector__and_PAMP_triggered_immunity_ L2 - https://doi.org/10.1111/mpp.12779 DB - PRIME DP - Unbound Medicine ER -