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Plants can produce reactive oxygen species (ROS) to counteract pathogen invasion, and pathogens have also evolved corresponding ROS scavenging strategies to promote infection and pathogenicity. Catalases (CATs) have been found to play pivotal roles in detoxifying H 2 O 2  formed by superoxide anion catalyzed by superoxide dismutases (SODs). However, few studies have addressed H 2 O 2  removing during rust fungi infection of wheat. In this study, we cloned a CAT gene  PsCAT1  from  Puccinia striiformis  f. sp.  tritici  ( Pst ), which encodes a monofunctional heme-containing catalase. PsCAT1 exhibited a high degree of tolerance to pH and temperature, and forms high homopolymers.  Heterologous complementation assays in  Saccharomyces cerevisiae  reveal that the signal peptide of PsCAT1 is functional. Overexpression of  PsCAT1  enhanced  S. cerevisiae  resistance to H 2 O 2 . Transient expression of  PsCAT1  in  Nicotiana benthamiana  suppressed Bax-induced cell death. Knockdown of  PsCAT1  using a host-induced gene silencing (HIGS) system led to the reduced virulence of  Pst , which was correlated to H 2 O 2  accumulation in HIGS plants. These results indicate that PsCAT1 acts as an important pathogenicity factor that facilitates  Pst  infection by scavenging host-derived H 2 O 2 .

A secreted catalase contributes to Puccinia striiformis resistance to host-derived oxidative stress