ArticleThe Journal of biological chemistry2026
Molecular mechanism of fungal effector PevD1-NRP interaction and discovery of a small-molecule disruptor.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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6 authors.
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Abstract
Verticillium wilt, caused by Verticillium dahliae, is a devastating vascular disease that severely affects cotton and other dicotyledonous crops worldwide. The fungal effector protein PevD1 promotes disease progression by interacting with the host asparagine-rich protein (NRP) and disrupting cryptochrome 2 (CRY2)-mediated signaling; however, the molecular basis of this interaction remains poorly understood. Here, we combined computational modeling, molecular interaction analysis, mutagenesis, and structural biology approaches to investigate the PevD1-NRP-CRY2 regulatory mechanism in Arabidopsis thaliana. AlphaFold-Multimer prediction and molecular dynamics (MD) simulations indicated that both PevD1 and the photolyase homology region of CRY2 interact with the death-associated domain of NRP through highly overlapping interfaces. Surface plasmon resonance and isothermal titration calorimetry analyses showed that PevD1 binds NRP with substantially higher affinity than CRY2 (K
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