Ya-Zhou Zhang 1,2,†, Qing Chen 2,†, Cai-Hong Liu 2, Lu Lei 2, Yang Li 2, Kan Zhao 2, Mei-Qiao Wei 2, Zhen-Ru Guo 2, Yan Wang 2, Bin-Jie Xu 2, Yun-Feng Jiang 2, Li Kong 2, Yan-Lin Liu 2, Xiu-Jin Lan 2, Qian-Tao Jiang 1,2, Jian Ma 2, Ji-Rui Wang 1,2, Guo-Yue Chen 1,2, Yu-Ming Wei 1,2,*, You-Liang Zheng 1,2 and Peng-Fei Qi 2,*
Fusarium graminearum causes Fusarium head blight (FHB), a devastating disease of wheat. Salicylic acid (SA) is involved in the resistance of wheat to F. graminearum. Cell wall mannoprotein (CWM) is known to trigger defense responses in plants, but its role in the pathogenicity of F. graminearum remains unclear. Here, we characterized FgCWM1 (FG05_11315), encoding a CWM in F. graminearum. FgCWM1 was highly expressed in wheat spikes by 24 h after initial inoculation and was upregulated by SA. Disruption of FgCWM1 (ΔFgCWM1) reduced mannose and protein accumulation in the fungal cell wall, especially under SA treatment, and resulted in defective fungal cell walls, leading to increased fungal sensitivity to SA. The positive role of FgCWM1 in mannose and protein accumulation was confirmed by its expression in Saccharomyces cerevisiae. Compared with wild type (WT), ΔFgCWM1 exhibited reduced pathogenicity toward wheat, but it produced the same amount of deoxynivalenol both in culture and in spikes. Complementation of ΔFgCWM1 with FgCWM1 restored the WT phenotype. Localization analyses revealed that FgCWM1 was distributed on the cell wall, consistent with its structural role. Thus, FgCWM1 encodes a CWM protein that plays an important role in the cell wall integrity and pathogenicity of F. graminearum.