Vibrio cholerae and Pseudomonas aeruginosa, along with other human pathogens, produce toxins that exhibit ADP-ribosyltransferase (ADP-RT) activity. This enzymatic function was first identified in a toxic protein from the plant pathogen Pseudomonas syringae, which causes leaf spot disease across various plant species. One of the key virulence factors secreted by this bacterium is HopU1, a protein delivered into host cells via the type III secretion system. Once inside, HopU1 targets the plant immune regulator AtGRP7, disrupting its function and making the plant more vulnerable to infection. Understanding how these mechanisms work could lead to the development of genetically modified crops with enhanced resistance to diseases. This discovery also raises intriguing evolutionary questions: while ADP-RT enzymes are well-known for their roles in animal systems, their presence and function in plants remain unclear. How did a pathogen acquire such a mechanism, and what are the implications for plant cellular processes? These findings open new doors for research into both plant immunity and the evolutionary origins of bacterial virulence strategies.
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