Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2021 Mar;115(3):412-424.
doi: 10.1111/mmi.14664. Epub 2020 Dec 29.

The structure and mechanism of the bacterial type II secretion system

Affiliations
Free article
Review

The structure and mechanism of the bacterial type II secretion system

Souvik Naskar et al. Mol Microbiol. 2021 Mar.
Free article

Abstract

The type II secretion system (T2SS) is a multi-protein complex used by many bacteria to move substrates across their cell membrane. Substrates released into the environment serve as local and long-range effectors that promote nutrient acquisition, biofilm formation, and pathogenicity. In both animals and plants, the T2SS is increasingly recognized as a key driver of virulence. The T2SS spans the bacterial cell envelope and extrudes substrates through an outer membrane secretin channel using a pseudopilus. An inner membrane assembly platform and a cytoplasmic motor controls pseudopilus assembly. This microreview focuses on the structure and mechanism of the T2SS. Advances in cryo-electron microscopy are enabling increasingly elaborate sub-complexes to be resolved. However, key questions remain regarding the mechanism of pseudopilus extension and retraction, and how this is coupled with the choreography of the substrate moving through the secretion system. The T2SS is part of an ancient type IV filament superfamily that may have been present within the last universal common ancestor (LUCA). Overall, mechanistic principles that underlie T2SS function have implication for other closely related systems such as the type IV and tight adherence pilus systems.

Keywords: assembly platform; cryo-EM; secretin; structure; type II secretion system; type IV pilus system.

PubMed Disclaimer

References

    1. Abendroth, J., Bagdasarian, M., Sandkvist, M. and Hol, W.G.J. (2004a) The structure of the cytoplasmic domain of EpsL, an inner membrane component of the type II secretion system of Vibrio cholerae: an unusual member of the actin-like ATPase superfamily. Journal of Molecular Biology, 344, 619-633.
    1. Abendroth, J., Kreger, A.C. and Hol, W.G.J. (2009a) The dimer formed by the periplasmic domain of EpsL from the type 2 secretion system of Vibrio parahaemolyticus. Journal of Structural Biology, 168, 313-322.
    1. Abendroth, J., Mitchell, D.D., Korotkov, K.V., Johnson, T.L., Kreger, A., Sandkvist, M. et al (2009b) The three-dimensional structure of the cytoplasmic domains of EpsF from the type 2 secretion system of Vibrio cholerae. Journal of Structural Biology, 166, 303-315.
    1. Abendroth, J., Murphy, P., Sandkvist, M., Bagdasarian, M. and Hol, W.G.J. (2005) The X-ray structure of the type II secretion system complex formed by the N-terminal domain of EpsE and the cytoplasmic domain of EpsL of Vibrio cholerae. Journal of Molecular Biology, 348, 845-855.
    1. Abendroth, J., Rice, A.E., McLuskey, K., Bagdasarian, M. and Hol, W.G.J. (2004b) The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold. Journal of Molecular Biology, 338, 585-596.

Publication types

MeSH terms

LinkOut - more resources