TY - JOUR
T1 - Discovery of a Novel Small-Molecule Inhibitor Targeting Myosin I to Control Colletotrichum siamense Anthracnose
AU - Liu, Songtao
AU - Liu, Fei
AU - Zhu, Xiyuan
AU - Zhang, Wanting
AU - Yang, Ziyang
AU - Li, Linwei
AU - Lei, Renkai
AU - Xu, Shu
AU - Yang, Shuai
AU - Li, Wangyang
AU - Chu, Xinyan
AU - Geng, Yiming
AU - Guo, Jingjing
AU - Chen, Yu
AU - Feng, Xu
AU - Zhang, Feng
N1 - Publisher Copyright:
© 2026 American Chemical Society
PY - 2026/7/22
Y1 - 2026/7/22
N2 - Anthracnose caused by Colletotrichum siamense severely impacts global crop and forest productivity. Here, we identify A22, a novel small-molecule inhibitor that targets C. siamense myosin I (CsMyoI), and this represents a previously untapped antifungal mechanism. Phenotypic screening, ATPase inhibition, and microscale thermophoresis (MST) confirmed that A22 binds to CsMyoI and disrupts its motor activity. Molecular dynamics simulations revealed stable interactions with the conserved phenamacril binding pocket, with a critical K379 substitution explaining species-specific differences in inhibitor sensitivity. Notably, A22 exhibited no cross-resistance with widely used fungicides, such as carbendazim or pyraclostrobin. In greenhouse trials, A22 outperformed the commercial fungicide prochloraz in controlling anthracnose on pepper, mango, and strawberry, even at low concentrations, and also promoted strawberry growth. These findings establish myosin I as a novel antifungal target and present A22 as a potent agent with a unique mode of action, offering a promising strategy for managing anthracnose and fungicide-resistant fungal strains.
AB - Anthracnose caused by Colletotrichum siamense severely impacts global crop and forest productivity. Here, we identify A22, a novel small-molecule inhibitor that targets C. siamense myosin I (CsMyoI), and this represents a previously untapped antifungal mechanism. Phenotypic screening, ATPase inhibition, and microscale thermophoresis (MST) confirmed that A22 binds to CsMyoI and disrupts its motor activity. Molecular dynamics simulations revealed stable interactions with the conserved phenamacril binding pocket, with a critical K379 substitution explaining species-specific differences in inhibitor sensitivity. Notably, A22 exhibited no cross-resistance with widely used fungicides, such as carbendazim or pyraclostrobin. In greenhouse trials, A22 outperformed the commercial fungicide prochloraz in controlling anthracnose on pepper, mango, and strawberry, even at low concentrations, and also promoted strawberry growth. These findings establish myosin I as a novel antifungal target and present A22 as a potent agent with a unique mode of action, offering a promising strategy for managing anthracnose and fungicide-resistant fungal strains.
KW - anthracnose
KW - antifungal agent
KW - Colletotrichum siamense
KW - myosin I inhibitor
KW - resistance management
UR - https://www.scopus.com/pages/publications/105045418372
U2 - 10.1021/acs.jafc.6c05881
DO - 10.1021/acs.jafc.6c05881
M3 - Article
C2 - 42441872
AN - SCOPUS:105045418372
SN - 0021-8561
VL - 74
SP - 21958
EP - 21971
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
IS - 28
ER -