Gram-negative bacterial pathogens interact with the host cells by using type III secretion systems (T3SS) to inject virulence proteins into cells. NleB effectors are glycosyltransferases that modify host protein substrates with N-acetyl glucosamine (GlcNAc) on arginine residues. This post-translational modification disrupts the normal functioning of host immune response proteins. T3SS effectors are thought to be inactive within the bacterium and fold into their active conformations after they are injected, due to the activity of chaperones . El Qaidi, et al (2020) reported that the bacterial glutathione synthetase (GshB) is glycosylated by NleB resulted in enhanced GshB activity, leading to an increase in glutathione production, and promoted bacterial survival in oxidative stress conditions. Is it possible that true role of T3SS effectors in bacteria was overlooked?

El Qaidi, S., Scott, N.E., Hays, M.P. et al. An intra-bacterial activity for a T3SS effector. Sci Rep 10, 1073 (2020). https://doi.org/10.1038/s41598-020-58062-y

(4) (PDF) An intra-bacterial activity for a T3SS effector (researchgate.net)

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