PlantView Supports Stripe Rust Resistance Research: Cellulose synthase TaCESA7 negatively regulates wheat resistance to stripe rust by reducing cell wall lignification

New progress has been made in research on wheat resistance to stripe rust.

Professor Kang Zhensheng and Professor Zhang Xinmei from Northwest A&F University published their findings in “ Stress Biology” (IF = 5.8)

This study uncovers a novel susceptibility mechanism underlying the wheat–stripe rust fungus interaction and provides new candidate targets and theoretical guidance for the molecular breeding of disease-resistant wheat.

Plants have evolved multiple constitutive and inducible defense mechanisms to combat pathogen invasion. As the first physical barrier against pathogens, the cell wall plays a pivotal role in plant immunity. In addition to providing structural protection, the cell wall can perceive external stresses and transmit signals that activate defense responses. Plant cell walls are classified into primary and secondary cell walls. Primary cell walls are mainly composed of cellulose, pectin, and hemicellulose, whereas secondary cell walls are enriched in cellulose, lignin, and xylan. Dynamic remodeling of their composition and structure is essential for regulating plant stress resistance. As the major load-bearing component of the cell wall, cellulose is synthesized by cellulose synthase (CESA) complexes (CSCs) located at the plasma membrane. The CESA protein family is highly conserved among plants, with different members specialized for cellulose biosynthesis in either primary or secondary cell walls. For example, AtCESA4, AtCESA7, and AtCESA8 are responsible for secondary cell wall cellulose synthesis in Arabidopsis. Multiple CESA genes have also been identified in crops such as maize and rice; however, functional studies of the CESA gene family in wheat remain limited.

Mutations or altered expression of CESA genes can affect cell wall integrity, thereby activating defense signaling pathways and either enhancing or reducing resistance to specific pathogens. For instance, Arabidopsis mutants defective in CESA3 exhibit increased resistance to multiple pathogens, whereas silencing cellulose synthesis-related genes in barley reduces resistance to powdery mildew. Reduced cellulose biosynthesis can also activate cell wall integrity pathways, inducing the expression of lignin biosynthesis genes and enhancing cell wall lignification. As a major component of secondary cell walls, lignin is synthesized through the phenylpropanoid pathway, and changes in lignin content can significantly influence disease-resistance phenotypes. Overexpression or knockout of lignin-related genes has been shown to alter plant susceptibility to fungal and bacterial pathogens.

Stripe rust, caused by Puccinia striiformis f. sp. tritici (Pst), is a devastating fungal disease that threatens global wheat production. However, the role of CESA genes in the wheat–Pst interaction has remained unclear. To address this question, the study focused on the Pst-responsive gene TaCESA7 and systematically investigated its biological function and regulatory mechanism. The researchers found that TaCESA7 is localized to the plasma membrane and participates in cellulose synthase complex assembly as a dimer. Overexpression of TaCESA7 reduced wheat resistance to Pst, whereas silencing or knockout of the gene enhanced broad-spectrum resistance to stripe rust by promoting lignin accumulation, activating defense-related gene expression, and increasing reactive oxygen species (ROS) production. Importantly, these improvements in disease resistance did not adversely affect major agronomic traits. The findings provide valuable candidate gene resources and theoretical support for the molecular breeding of fungal disease-resistant wheat.

Experiments using Plantview

The study utilized the PlantView Multimodal Plant In Vivo Imaging System developed by Biolight Biotechnology to examine the interactions between TaCESA7 and TaCESA7, as well as between TaCESA7 and TaCESA8, in Nicotiana benthamiana leaves. The results demonstrated that TaCESA7 exhibits both self-interaction and heterodimerization with TaCESA8.

DOI: 10.1007/s44154-025-00244-7