The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
ESAT-6 from Mycobacterium tuberculosis Dissociates from Its Putative Chaperone CFP-10 under Acidic Conditions and Exhibits Membrane-Lysing Activity
Open accessAbstract
The 6-kDa early secreted antigenic target ESAT-6 and the 10-kDa culture filtrate protein CFP-10 of Mycobacterium tuberculosis are secreted by the ESX-1 system into the host cell and thereby contribute to pathogenicity. Although different studies performed at the organismal and cellular levels have helped to explain ESX-1-associated phenomena, not much is known about how ESAT-6 and CFP-10 contribute to pathogenesis at the molecular level. In this study we describe the interaction of both proteins with lipid bilayers, using biologically relevant liposomal preparations containing dimyristoylphosphatidylcholine (DMPC), dimyristoylphosphatidylglycerol, and cholesterol. Using floatation gradient centrifugation, we demonstrate that ESAT-6 showed strong association with liposomes, and in particular with preparations containing DMPC and cholesterol, whereas the interaction of CFP-10 with membranes appeared to be weaker and less specific. Most importantly, binding to the biomembranes no longer occurred when the proteins were present as a 1:1 ESAT-6·CFP-10 complex. However, lowering of the pH resulted in dissociation of the protein complex and subsequent protein-liposome interaction. Finally, cryoelectron microscopy revealed that ESAT-6 destabilized and lysed liposomes, whereas CFP-10 did not. In conclusion, we propose that one of the main features of ESAT-6 in the infection process of M. tuberculosis is the interaction with biomembranes that occurs after dissociation from its putative chaperone CFP-10 under acidic conditions typically encountered in the phagosome.
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Cites
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Type VII secretion — mycobacteria show the way
Abdallah, A. M., Gey van Pittius, N. C., DiGiuseppe Champion, P. A., Cox, J., Luirink, J., Vandenbroucke-Grauls, C. M. J. E., Appelmelk, B. J., & Bitter, W. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1773 · Cited by 763
Phagosomal Rupture by Mycobacterium tuberculosis Results in Toxicity and Host Cell Death
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Tuberculous Granuloma Induction via Interaction of a Bacterial Secreted Protein with Host Epithelium
Volkman, H. E., Pozos, T. C., Zheng, J., Davis, J. M., Rawls, J. F., & Ramakrishnan, L. (2010) · Science · doi:10.1126/science.1179663 · Cited by 448
Metadata
- Authors
- de Jonge, M. I., Pehau-Arnaudet, G., Fretz, M. M., Romain, F., Bottai, D., Brodin, P., Honoré, N., Marchal, G., Jiskoot, W., England, P., Cole, S. T., & Brosch, R.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2007-08-15
- Volume
- 189
- Issue
- 16
- Pages
- 6028-6034
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- OpenAlex
- W2161794466
- Cited by
- 326
- References
- 52
- FWCI
- 8.62
- Type
- journal article
- Language
- en
- Open access
- green
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- de Jonge, M. I., Pehau-Arnaudet, G., Fretz, M. M., Romain, F., Bottai, D., Brodin, P., Honoré, N., Marchal, G., Jiskoot, W., England, P., Cole, S. T., & Brosch, R. (2007). ESAT-6 from Mycobacterium tuberculosis Dissociates from Its Putative Chaperone CFP-10 under Acidic Conditions and Exhibits Membrane-Lysing Activity. Journal of Bacteriology. https://doi.org/10.1128/jb.00469-07
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
