FvLcp1, a type-D fungal LysM protein with Chitin-binding domains, is a secreted protein involved in host recognition and fumonisin production in Fusarium verticillioides - maize kernel interaction

摘要: SUMMARY Fusarium verticillioides is one of the key maize ear rot pathogens and produces fumonisins, a group mycotoxins detrimental to humans animals. Unfortunately, our understanding on how this fungus interacts with kernels trigger mycotoxin biosynthesis very limited. We performed systematic computational network-based analysis large-scale F. RNA-seq datasets identify potential gene subnetwork modules that are associated virulence fumonisin regulation. Among highly discriminative modules, we identified putative hub FvLCP1, which encodes type-D fungal LysM protein signal peptide, three domains, two chitin binding domains. FvLcp1 unique harbors these domains amongst five representative species. secreted important for production domain playing acritical role. Chitin-binding was essential in vitro binding. Using rice blast fungus, learned accumulates appressoria, infection structure, suggesting could be involved host recognition infection. Also, full length able suppress BAX triggered plant cell death Nicotiana benthamiana. This first report where chitin-binding mycotoxigenic shown potentially suppressing promoting fumonisins while pathogen colonizes kernels.