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The  Valsa  canker, caused by  Valsa mali  ( V. mali ), is a destructive disease of apple in Eastern Asia. Effector proteins are important for fungal pathogenicity. We studied a candidate effector VmPxE1 isolated based on the genome information of  V. mali.  By using the yeast invertase secretion assay system, VmPxE1 was shown to contain a signal peptide with secretory functions. VmPxE1 can suppress BCL-2-associated X protein (BAX)-induced cell death with a high efficacy of 92% in  Nicotiana benthamiana . The expression of  VmPxE1  was upregulated during the early infection stage and deletion of  VmPxE1  led to significant reductions in virulence on both apple twigs and leaves. VmPxE1 was also shown to target an apple ascorbate peroxidase (MdAPX1) by the yeast two-hybrid screening, bimolecular fluorescence complementation and  in vivo  co-immunoprecipitation. Sequence phylogenetic analysis suggested that MdAPX1 was an ascorbate peroxidase belonging to a subgroup of heme-dependent peroxidases of the plant superfamily. The ectopic expression of  MdAPX1  in the mutant of  VmPxE1  significantly enhanced resistance to H 2 O 2 , while the presence of  VmPxE1  seems to disturb  MdAPX1  function. The present results provide insights into the functions of VmPxE1 as a candidate effector of  V. mali  in causing apple canker.

Valsa mali Pathogenic Effector VmPxE1 Contributes to Full Virulence and Interacts With the Host Peroxidase MdAPX1 as a Potential Target