RBB1 negatively regulates rice disease resistance by modulating protein glycosylation

Glycosylation, a prevalent post-translational modification in eukaryotic secreted and membrane-associated proteins, plays a pivotal role in diverse physiological and pathological processes. Although UDP-N-acetylglucosamine (UDP-GlcNAc) is essential for this modification, the specific glycosylation mechanisms during plant leaf senescence and defense responses remain poorly understood. In our research, we identified a novel rice mutant named rbb1 (resistance to blast and bacterial blight1), exhibiting broad-spectrum disease resistance. This mutant phenotype results from a loss-of-function mutation in the gene encoding glucosamine-6-phosphate acetyltransferase, an important enzyme in D-glucosamine 6-phosphate acetylation. The rbb1 mutant demonstrates enhanced defense responses, evident in increased resistance to rice blast and bacterial blight, along with the upregulation of defense-response genes. Various biochemical markers indicate an activated defense mechanism in the rbb1 mutant, such as elevated levels of reactive oxygen species and malondialdehyde, reduced enzyme activity and UDP-GlcNAc content, and decreased expression of N-glycan and O-glycan modifying proteins. Moreover, proteome analysis of N-glycosylation modifications reveals alterations in the N-glycosylation of several disease-resistance-related proteins, with a significant reduction in Prx4 and Prx13 in rbb1-1. Additionally, the knockout of Prx4 or Prx13 also enhances resistance to Xanthomonas oryzae pv. oryzae (Xoo) and Magnaporthe oryzae (M. oryzae). This study uncovers a novel mechanism of defense response in rice, suggesting potential targets for the development of disease-resistant varieties.