Mycobacterial type VII secretion systems-Reference-Cited by-同舟云学术

Mycobacterial type VII secretion systems

Published:2023-06-01 Issue:7 Volume:404 Page:691-702
ISSN:1431-6730
Container-title:Biological Chemistry
language:en
Short-container-title:

Author:

Famelis Nikolaos¹^ORCID,Geibel Sebastian²^ORCID,van Tol Daan²

Affiliation:

1. Institute for Molecular Infection Biology, Julius Maximilian University of Würzburg , D-97080 Würzburg , Germany

2. Leiden Institute of Chemistry, Leiden University , NL-2333 CC Leiden , Netherlands

Abstract

Abstract Mycobacteria, such as the pathogen M. tuberculosis, utilize up to five paralogous type VII secretion systems to transport proteins across their cell envelope. Since these proteins associate in pairs that depend on each other for transport to a different extent, the secretion pathway to the bacterial surface remained challenging to address. Structural characterization of the inner-membrane embedded secretion machineries along with recent advances on the substrates’ co-dependencies for transport allow for the first time more detailed and testable models for secretion.

Publisher

Walter de Gruyter GmbH

Subject

Clinical Biochemistry,Molecular Biology,Biochemistry

Link

https://www.degruyter.com/document/doi/10.1515/hsz-2022-0350/pdf

Reference74 articles.

1. Ates, L.S., Ummels, R., Commandeur, S., Van De Weerd, R., Sparrius, M., Weerdenburg, E., Alber, M., Kalscheuer, R., Piersma, S.R., Abdallah, A.M., et al.. (2015). Essential role of the ESX-5 secretion system in outer membrane permeability of pathogenic mycobacteria. PLoS Genet. 11: e1005190, https://doi.org/10.1371/journal.pgen.1005190.

2. Ates, L.S. (2020). New insights into the mycobacterial PE and PPE proteins provide a framework for future research. Mol. Microbiol. 113: 4–21, https://doi.org/10.1111/mmi.14409.

3. Augenstreich, J., Arbues, A., Simeone, R., Haanappel, E., Wegener, A., Sayes, F., Le Chevalier, F., Chalut, C., Malaga, W., Guilhot, C., et al. (2017). ESX-1 and phthiocerol dimycocerosates of Mycobacterium tuberculosis act in concert to cause phagosomal rupture and host cell apoptosis. Cell. Microbiol. 19: e12726, https://doi.org/10.1111/cmi.12726.

4. Babu Sait, M.R., Koliwer-Brandl, H., Stewart, J.A., Swarts, B.M., Jacobsen, M., Ioerger, T.R., and Kalscheuer, R. (2022). PPE51 mediates uptake of trehalose across the mycomembrane of Mycobacterium tuberculosis. Sci. Rep. 12: 2097, https://doi.org/10.1038/s41598-022-06109-7.

5. Beckham, K.S., Ciccarelli, L., Bunduc, C.M., Mertens, H.D., Ummels, R., Lugmayr, W., Mayr, J., Rettel, M., Savitski, M.M., Svergun, D.I., et al.. (2017). Structure of the mycobacterial ESX-5 type VII secretion system membrane complex by single-particle analysis. Nat. Microbiol. 2: 17047, https://doi.org/10.1038/nmicrobiol.2017.47.

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