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The ability of human enteric pathogens to colonize plants and use them as alternate hosts is now well established.  Salmonella , similarly to phytobacteria, appears to be capable of producing the plant hormone auxin via an indole-3-pyruvate decarboxylase (IpdC), a key enzyme of the IPyA pathway. A deletion of the  Salmonella ipdC  significantly reduced auxin synthesis in laboratory culture. The  Salmonella ipdC  gene was expressed on root surfaces of  Medicago truncatula .  M. truncatula  auxin-responsive  GH3::GUS  reporter was activated by the wild type  Salmonella , and not but the  ipdC  mutant, implying that the bacterially produced IAA (Indole Acetic Acid) was detected by the seedlings. Seedling infections with the wild type  Salmonella  caused an increase in secondary root formation, which was not observed in the  ipdC  mutant. The wild type  Salmonella  cells were detected as aggregates at the sites of lateral root emergence, whereas the  ipdC  mutant cells were evenly distributed in the rhizosphere. However, both strains appeared to colonize seedlings well in growth pouch experiments. The  ipdC  mutant was also less virulent in a murine model of infection. When mice were infected by oral gavage, the  ipdC  mutant was as proficient as the wild type strain in colonization of the intestine, but it was defective in the ability to cross the intestinal barrier. Fewer cells of the  ipdC  mutant, compared with the wild type strain, were detected in Peyer's patches, spleen and in the liver. Orthologs of  ipdC  are found in all  Salmonella  genomes and are distributed among many animal pathogens and plant-associated bacteria of the  Enterobacteriaceae , suggesting a broad ecological role of the IpdC-catalyzed pathway.

Production of the Plant Hormone Auxin by Salmonella and Its Role in the Interactions with Plants and Animals