Pseudomonas aeruginosa T6SS-mediated molybdate transport contributes to bacterial competition during anaerobiosis

Type VI secretion system (T6SS) is widely distributed in Gram-negative bacteria and functions as a versatile protein export machinery that translocates effectors into eukaryotic or prokaryotic target cells. Growing evidence indicates that T6SS can deliver several effectors to promote bacterial survival in harmful environments through metal ion acquisition. Here, we report that the Pseudomonas aeruginosa H2-T6SS mediates molybdate (MoO42-) acquisition by secretion of a molybdate-binding protein, ModA. The expression of H2-T6SS genes is activated by the master regulator Anr and anaerobiosis. We also identified a ModA-binding protein, IcmP, an insulin-cleaving metalloproteinase outer membrane protein. The T6SS-ModA-IcmP system provides P. aeruginosa with a growth advantage in bacterial competition under anaerobic conditions and plays an important role in bacterial virulence. Overall, this study clarifies the role of T6SS in secretion of an anion-binding protein, emphasizing the fundamental importance of this bacterium using T6SS-mediated molybdate uptake to adapt to complex environmental conditions.

Automated summary

The Type VI secretion system (T6SS) in Gram-negative bacteria serves as a versatile protein export machinery for translocating effectors into target cells, promoting bacterial survival in harmful environments. This study demonstrates that Pseudomonas aeruginosa H2-T6SS mediates molybdate acquisition by secreting a molybdate-binding protein ModA, providing a growth advantage in bacterial competition under anaerobic conditions. The findings highlight the fundamental importance of T6SS in helping bacteria adapt to complex environmental conditions through metal ion uptake.