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

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). SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s44154-021-00021-2.