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Porins in the Cell Wall of Mycobacteria
Abstract
The cell wall of mycobacteria is an efficient permeability barrier that makes mycobacteria naturally resistant to most antibiotics. Liposome swelling assays and planar bilayer experiments were used to investigate the diffusion process of hydrophilic molecules through the cell wall of Mycobacterium chelonae and identify the main hydrophilic pathway. A 59-kilodalton cell wall protein formed a water-filled channel with a diameter of 2.2 nanometers and an average single-channel conductance equal to 2.7 nanosiemens in 1 M potassium chloride. These results suggest that porins can be found in the cell wall of a Gram-positive bacterium. A better knowledge of the hydrophilic pathways should help in the design of more effective antimycobacterial agents.
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Cited by
Molecular Basis of Bacterial Outer Membrane Permeability Revisited
Nikaido, H. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.4.593-656.2003 · Cited by 4,316
Prevention of Drug Access to Bacterial Targets: Permeability Barriers and Active Efflux
Nikaido, H. (1994) · Science · doi:10.1126/science.8153625 · Cited by 1,540
Non-tuberculous mycobacteria and the rise of Mycobacterium abscessus
Johansen, M. D., Herrmann, J.-L., & Kremer, L. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-020-0331-1 · Cited by 822
The Envelope Layers of Mycobacteria with Reference to their Pathogenicity
Daffé, M., & Draper, P. (1997) · Advances in Microbial Physiology · doi:10.1016/s0065-2911(08)60016-8 · Cited by 730
Mycobacterial cell wall: Structure and role in natural resistance to antibiotics
Jarlier, V (1994) · FEMS Microbiology Letters · doi:10.1016/0378-1097(94)90267-4 · Cited by 593
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Metadata
- Authors
- Trias, J., Jarlier, V., & Benz, R.
- Venue
- Science
- Published
- 1992-11-27
- Volume
- 258
- Issue
- 5087
- Pages
- 1479-1481
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2038031211
- Cited by
- 222
- References
- 0
- FWCI
- 6.38
- Type
- journal article
- Language
- en
- Open access
- closed
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