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Fusarium graminearum  is a destructive wheat pathogen. No fully resistant cultivars are available. Knowledge concerning the molecular weapons of  F. graminearum  to achieve infection remains limited. Here, we report that deletion of the putative secondary metabolite biosynthesis gene cluster  fg3_54  compromises the pathogen’s ability to infect wheat through cell-to-cell penetration. Ectopic expression of  fgm4 , a pathway-specific bANK-like regulatory gene, activates the transcription of the  fg3_54  cluster in vitro. We identify a linear, C- terminally reduced and  d -amino acid residue-rich octapeptide, fusaoctaxin A, as the product of the two nonribosomal peptide synthetases encoded by  fg3_54 . Chemically-synthesized fusaoctaxin A restores cell-to-cell invasiveness in  fg3_54 -deleted  F. graminearum , and enables colonization of wheat coleoptiles by two  Fusarium  strains that lack the  fg3_54  homolog and are nonpathogenic to wheat. In conclusion, our results identify fusaoctaxin A as a virulence factor required for cell-to-cell invasion of wheat by  F. graminearum .

A linear nonribosomal octapeptide from Fusarium graminearum facilitates cell-to-cell invasion of wheat