LACCASE35 enhances lignification and resistance against Pseudomonas syringae pv. actinidiae infection in kiwifruit.

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Tác giả: Fuxi Bai, Zemin Fang, Lili Huang, Rui Li, Yawei Li, Pu Liu, Wei Liu, Xiaojie Wang, Shunyuan Wu, Dongle Zhang, Rongrong Zhou

Ngôn ngữ: eng

Ký hiệu phân loại: 633.14 *Rye

Thông tin xuất bản: United States : Plant physiology , 2025

Mô tả vật lý:

Bộ sưu tập: NCBI

ID: 160671

Kiwifruit bacterial canker, a highly destructive disease caused by Pseudomonas syringae pv. actinidiae (Psa), seriously affects kiwifruit (Actinidia spp.) production. Lignin deposition in infected cells serves as a defense mechanism, effectively suppressing pathogen growth. However, the underlying process remains unclear. In this study, we determined that Psa infection leads to a significant increase in S-lignin accumulation in kiwifruit. The S/G ratio in lignin was higher in a Psa-resistant cultivar than in a Psa-sensitive cultivar. Furthermore, kiwifruit laccase 35 (AcLac35), encoding an enzyme in the lignin biosynthesis pathway with characteristic laccase activity, showed tissue-specific expression in plants and was upregulated following infection by Psa. Overexpressing AcLac35 in kiwifruit leaves resulted in greater lignin content than in wild-type leaves, leading to the formation of thicker cell walls, and also activated plant-pathogen interactions and MAPK pathways, thereby enhancing resistance against Psa infection. Yeast 1-hybrid assays, dual-LUC reporter assays, electrophoretic mobility shift assays, and transient injection experiments indicated that SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE 9 (AcSPL9) can bind to the AcLac35 promoter, thereby positively regulating its expression. Moreover, overexpression of AcSPL9 increased lignin accumulation in kiwifruit leaves, enhancing resistance to Psa, while virus-induced gene silencing of AcSPL9 expression reduced this resistance. Our findings reveal the function of AsSPL9-AcLac35 in kiwifruit, providing insight into enhancing resistance against Psa in kiwifruit.
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