ArticleBMC research notes2026
The M91 metallopeptidase domain of the T6SS effector protein SED_RS06335 encoded in Salmonella Dublin SPI-19 exhibits antibacterial activity.
Article in BMC research notes, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
objectiveThe Type VI Secretion System (T6SS) is a contractile apparatus made of several proteins playing a significant role in the fitness and virulence of many Gram-negative bacteria. The SPI-19 T6SS gene cluster is a virulence factor of Salmonella Dublin contributing to host colonization and antibacterial activity. Previously, we demonstrated that SED_RS06335 (an Rhs protein with a C-terminal M91 domain) is responsible for antibacterial activity of the T6SS
resultsHere, we determine through interbacterial competition and heterologous expression assays that M91 domain of SED_RS06335 displays antibacterial activity. Furthermore, a three-dimensional structural model of M91 domain revealed a high similarity with the metallopeptidase neurotoxin type A (BotA) from Clostridium botulinum. Interestingly, our results suggest that the M91 domain is responsible for the antibacterial activity of the SED_RS06335 effector in Salmonella Dublin.
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