Functional diversification of CsCAD14 orchestrates synergistic phenylpropanoid biosynthesis to defend gray blight disease in tea plants
- 1State Key Laboratory for Tea Plant Germplasm Innovation and Resource Utilization/ Key Laboratory of Tea Biology and Tea Processing of Ministry of Agriculture and rural affairs, Anhui Agricultural University, West 130 Changjiang Road, Hefei 230036, Anhui, China.
- 2Department of Plant and Microbial Biology, North Carolina State University, Raleigh, NC 27695, USA.
- 3Rizhao Lanshan Tea Co., Ltd., Rizhao 276800, China.
Abstract
Phenylpropanoid metabolism is a crucial secondary metabolic pathway in plants. Numerous neofunctionalized and specialized enzymes emerged during plant terrestrialization, yielding metabolites contributing to environmental adaptation. Here, a cinnamyl alcohol dehydrogenase from tea plant ( Camellia sinensis ), CsCAD14, exhibited dual activity catalyzing monolignol and hydroxycinnamic acid biosynthesis. Antifungal assays showed that monolignols and hydroxycinnamic acids synergistically inhibited Pestalotiopsis growth. Integrated functional characterizations revealed that CsCAD14 enhanced gray blight disease resistance by increasing monolignol and hydroxycinnamic acid levels compared to CsCAD11 featured with single-enzymatic activity. Notably, genetic analysis of F 1 progeny from crossing susceptible and resistant tea cultivars identified a nonsynonymous mutation in the CsCAD14 coding region, which abolished dual-enzymatic activity and was associated with pathogen susceptibility. Furthermore, evolutionary analysis revealed a positively selected amino acid substitution (L192V) driving CAD functional diversification from single-enzymatic activity in algae to dual-enzymatic activity in land plants. These findings uncover neofunctionalization of dual-activity CADs evolved for phenylpropanoid defense to enhance fungal disease resistance during plant adaptation to terrestrial environments.
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BibTeX
@article{xu2026functional,
title = {{Functional diversification of CsCAD14 orchestrates synergistic phenylpropanoid biosynthesis to defend gray blight disease in tea plants}},
author = {Linlin Xu and Songyan Huang and Jie Deng and Chunmiao Zhang and Jing Yang and Mengsha Tang and Lingyao Luo and Hongrong Chen and Shengrui Liu and De-yu Xie and Zuojia Zhang and Chaoling Wei and Junyan Zhu},
journal = {Science Advances},
year = {2026},
month = oct,
doi = {10.1126/sciadv.aei1647},
url = {https://www.science.org/doi/10.1126/sciadv.aei1647},
note = {CC BY-NC},
}
RIS
TY - JOUR
TI - Functional diversification of CsCAD14 orchestrates synergistic phenylpropanoid biosynthesis to defend gray blight disease in tea plants
AU - Linlin Xu
AU - Songyan Huang
AU - Jie Deng
AU - Chunmiao Zhang
AU - Jing Yang
AU - Mengsha Tang
AU - Lingyao Luo
AU - Hongrong Chen
AU - Shengrui Liu
AU - De-yu Xie
AU - Zuojia Zhang
AU - Chaoling Wei
AU - Junyan Zhu
PY - 2026
DA - 2026/10/02
JO - Science Advances
DO - 10.1126/sciadv.aei1647
UR - https://www.science.org/doi/10.1126/sciadv.aei1647
AB - Phenylpropanoid metabolism is a crucial secondary metabolic pathway in plants. Numerous neofunctionalized and specialized enzymes emerged during plant terrestrialization, yielding metabolites contributing to environmental adaptation. Here, a cinnamyl alcohol dehydrogenase from tea plant ( Camellia sinensis ), CsCAD14, exhibited dual activity catalyzing monolignol and hydroxycinnamic acid biosynthesis. Antifungal assays showed that monolignols and hydroxycinnamic acids synergistically inhibited Pestalotiopsis growth. Integrated functional characterizations revealed that CsCAD14 enhanced gray blight disease resistance by increasing monolignol and hydroxycinnamic acid levels compared to CsCAD11 featured with single-enzymatic activity. Notably, genetic analysis of F 1 progeny from crossing susceptible and resistant tea cultivars identified a nonsynonymous mutation in the CsCAD14 coding region, which abolished dual-enzymatic activity and was associated with pathogen susceptibility. Furthermore, evolutionary analysis revealed a positively selected amino acid substitution (L192V) driving CAD functional diversification from single-enzymatic activity in algae to dual-enzymatic activity in land plants. These findings uncover neofunctionalization of dual-activity CADs evolved for phenylpropanoid defense to enhance fungal disease resistance during plant adaptation to terrestrial environments.
SN - 2375-2548
ER -