The DOI matches its Crossref record.
THE ENVELOPE OF MYCOBACTERIA
Abstract
Mycobacteria, members of which cause tuberculosis and leprosy, produce cell walls of unusually low permeability, which contribute to their resistance to therapeutic agents. Their cell walls contain large amounts of C 60-C 90 fatty acids, mycolic acids, that are covalently linked to arabinogalactan. Recent studies clarified the unusual structures of arabinogalactan as well as of extractable cell wall lipids, such as trehalose-based lipooligosaccharides, phenolic glycolipids, and glycopeptidolipids. Most of the hydrocarbon chains of these lipids assemble to produce an asymmetric bilayer of exceptional thickness. Structural considerations suggest that the fluidity is exceptionally low in the innermost part of bilayer, gradually increasing toward the outer surface. Differences in mycolic acid structure may affect the fluidity and permeability of the bilayer, and may explain the different sensitivity levels of various mycobacterial species to lipophilic inhibitors. Hydrophilic nutrients and inhibitors, in contrast, traverse the cell wall presumably through channels of recently discovered porins.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
Self-citationA comprehensive classification system for lipids
Fahy, E., Subramaniam, S., Brown, H. A., Glass, C. K., Merrill, A. H., Murphy, R. C., Raetz, C. R. H., Russell, D. W., Seyama, Y., Shaw, W., et al. (2005) · Journal of Lipid Research · doi:10.1194/jlr.e400004-jlr200 · Cited by 1,699
Mycobacterium tuberculosis Pathogenesis and Molecular Determinants of Virulence
Smith, I. (2003) · Clinical Microbiology Reviews · doi:10.1128/cmr.16.3.463-496.2003 · Cited by 1,154
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
Peyron, P., Vaubourgeix, J., Poquet, Y., Levillain, F., Botanch, C., Bardou, F., Daffé, M., Emile, J.-F., Marchou, B., Cardona, P.-J., et al. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000204 · Cited by 751
Role of the Major Antigen of Mycobacterium tuberculosis in Cell Wall Biogenesis
Belisle, J. T., Vissa, V. D., Sievert, T., Takayama, K., Brennan, P. J., & Besra, G. S. (1997) · Science · doi:10.1126/science.276.5317.1420 · Cited by 734
Self-citationEssential Role for Cholesterol in Entry of Mycobacteria into Macrophages
Gatfield, J., & Pieters, J. (2000) · Science · doi:10.1126/science.288.5471.1647 · Cited by 615
Hoffmann, C., Leis, A., Niederweis, M., Plitzko, J. M., & Engelhardt, H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709530105 · Cited by 596
Tetracyclines: Antibiotic action, uptake, and resistance mechanisms
Schnappinger, D., & Hillen, W. (1996) · Archives of Microbiology · doi:10.1007/s002030050339 · Cited by 484
Belanger, A. E., Besra, G. S., Ford, M. E., Mikusová, K., Belisle, J. T., Brennan, P. J., & Inamine, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11919 · Cited by 466
Self-citationDirect Visualization of the Outer Membrane of Mycobacteria and Corynebacteria in Their Native State
Zuber, B., Chami, M., Houssin, C., Dubochet, J., Griffiths, G., & Daffé, M. (2008) · Journal of Bacteriology · doi:10.1128/jb.01919-07 · Cited by 458
Bacterial Growth and Cell Division: a Mycobacterial Perspective
Hett, E. C., & Rubin, E. J. (2008) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00028-07 · Cited by 408
The mycobacterial cell envelope — a moving target
Dulberger, C. L., Rubin, E. J., & Boutte, C. C. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-019-0273-7 · Cited by 365
Crystal Structures of Membrane Transporter MmpL3, an Anti-TB Drug Target
Zhang, B., Li, J., Yang, X., Wu, L., Zhang, J., Yang, Y., Zhao, Y., Zhang, L., Yang, X., Yang, X., et al. (2019) · Cell · doi:10.1016/j.cell.2019.01.003 · Cited by 263
Augenstreich, J., Arbues, A., Simeone, R., Haanappel, E., Wegener, A., Sayes, F., Le Chevalier, F., Chalut, C., Malaga, W., Guilhot, C., et al. (2017) · Cellular Microbiology · doi:10.1111/cmi.12726 · Cited by 240
Bottai, D., Di Luca, M., Majlessi, L., Frigui, W., Simeone, R., Sayes, F., Bitter, W., Brennan, M. J., Leclerc, C., Batoni, G., et al. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08001.x · Cited by 210
The Macrophage: A Disputed Fortress in the Battle against Mycobacterium tuberculosis
Queval, C. J., Brosch, R., & Simeone, R. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02284 · Cited by 215
MmpL3 is the flippase for mycolic acids in mycobacteria
Xu, Z., Meshcheryakov, V. A., Poce, G., & Chng, S.-S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1700062114 · Cited by 201
Rao, V. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27335 · Cited by 200
Ates, L. S., Ummels, R., Commandeur, S., van der Weerd, R., Sparrius, M., Weerdenburg, E., Alber, M., Kalscheuer, R., Piersma, S. R., Abdallah, A. M., et al. (2015) · PLOS Genetics · doi:10.1371/journal.pgen.1005190 · Cited by 185
MmpL3 is a lipid transporter that binds trehalose monomycolate and phosphatidylethanolamine
Su, C.-C., Klenotic, P. A., Bolla, J. R., Purdy, G. E., Robinson, C. V., & Yu, E. W. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1901346116 · Cited by 148
Thammahong, A., Puttikamonkul, S., Perfect, J. R., Brennan, R. G., & Cramer, R. A. (2017) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00053-16 · Cited by 125
Puech, V., Guilhot, C., Perez, E., Tropis, M., Armitige, L. Y., Gicquel, B., & Daffé, M. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02953.x · Cited by 121
Molle, V., Brown, A. K., Besra, G. S., Cozzone, A. J., & Kremer, L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601691200 · Cited by 111
Nguyen, L., Chinnapapagari, S., & Thompson, C. J. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.19.6603-6611.2005 · Cited by 108
Stress response in rhodococcus strains
Pátek, M., Grulich, M., & Nešvera, J. (2021) · Biotechnology Advances · doi:10.1016/j.biotechadv.2021.107698 · Cited by 106
Imaging mycobacterial growth and division with a fluorogenic probe
Hodges, H. L., Brown, R. A., Crooks, J. A., Weibel, D. B., & Kiessling, L. L. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1720996115 · Cited by 96
Veyron-Churlet, R., Zanella-Cléon, I., Cohen-Gonsaud, M., Molle, V., & Kremer, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.105189 · Cited by 80
Esx Systems and the Mycobacterial Cell Envelope: What's the Connection?
Bosserman, R. E., & Champion, P. A. (2017) · Journal of Bacteriology · doi:10.1128/jb.00131-17 · Cited by 42
Minnikin, D. E., Lee, O. Y.-C., Wu, H. H. T., Nataraj, V., Donoghue, H. D., Ridell, M., Watanabe, M., Alderwick, L., Bhatt, A., & Besra, G. S. (2015) · Tuberculosis - Expanding Knowledge · doi:10.5772/59585 · Cited by 43
Mishra, N., Tiwari, V. K., & Schmidt, R. R. (2020) · Carbohydrates in Drug Discovery and Development · doi:10.1016/b978-0-12-816675-8.00001-4 · Cited by 17
Lin, E.-C., Tu, H.-P., & Hong, C.-H. (2023) · Respiratory Research · doi:10.1186/s12931-023-02365-x · Cited by 13
Adaptation of Rhodococcus to organic solvents
de Carvalho, C. C. C. R. (2019) · Microbiology Monographs · doi:10.1007/978-3-030-11461-9_5 · Cited by 12
Oloya, B., Namukobe, J., Heydenreich, M., Ssengooba, W., Schmidt, B., & Byamukama, R. (2021) · Natural Product Communications · doi:10.1177/1934578x211035851 · Cited by 9
Metadata
- Authors
- Brennan, P. J., & Nikaido, H.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 1995-06
- Volume
- 64
- Issue
- 1
- Pages
- 29-63
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2140981202
- Cited by
- 1,985
- References
- 0
- FWCI
- 31.26
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
