The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Tetracycline antibiotics and resistance mechanisms
Abstract
The ribosome and protein synthesis are major targets within the cell for inhibition by antibiotics, such as the tetracyclines. The tetracycline family of antibiotics represent a large and diverse group of compounds, ranging from the naturally produced chlortetracycline, introduced into medical usage in the 1940s, to second and third generation semi-synthetic derivatives of tetracycline, such as doxycycline, minocycline and more recently the glycylcycline tigecycline. Here we describe the mode of interaction of tetracyclines with the ribosome and mechanism of action of this class of antibiotics to inhibit translation. Additionally, we provide an overview of the diverse mechanisms by which bacteria obtain resistance to tetracyclines, ranging from efflux, drug modification, target mutation and the employment of specialized ribosome protection proteins.
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“The most common efflux pump genes, tet(K) and tet(L), encode membrane-associated proteins that actively transport tetracycline out of the bacterial cell, reducing intracellular drug concentration and thereby limiting its efficacy [249,254,255].”
From Staphylococcus aureus: A Review of the Pathogenesis and Virulence Mechanisms (2025) · cites this paper as [255]
In the citing paper
“Resistance to tetracyclines in S. aureus primarily occurs through active efflux pumps and ribosomal protection proteins.”
From Staphylococcus aureus: A Review of the Pathogenesis and Virulence Mechanisms (2025) · cites this paper as [255]
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Cites
Brodersen, D. E., Clemons, W. M., Carter, A. P., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Cell · doi:10.1016/s0092-8674(00)00216-6 · Cited by 950 · cited 4×
“The binding site of tetracycline on the 30S subunit and 70S ribosome X-ray structures of tetracycline in complex with the Thermus thermophilus 30S subunit provided the first direct visualization of the drug binding sites (Figure 2A) (Brodersen et al., 2000; Pioletti et al., 2001).”
BackgroundMethodInfluentialRoberts, M. C. (1996) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1996.tb00251.x · Cited by 689
Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3
Pioletti, M., Schlünzen, F., Harms, J., Zarivach, R., Glühmann, M., Avila, H., Bashan, A., Bartels, H., Auerbach, T., Jacobi, C., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.8.1829 · Cited by 527
The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State
Gao, Y.-G., Selmer, M., Dunham, C. M., Weixlbaumer, A., Kelley, A. C., & Ramakrishnan, V. (2009) · Science · doi:10.1126/science.1179709 · Cited by 513
MECHANISMS UNDERLYING EXPRESSION OF TN 10 ENCODED TETRACYCLINE RESISTANCE
Hillen, W., & Berens, C. (1994) · Annual Review of Microbiology · doi:10.1146/annurev.mi.48.100194.002021 · Cited by 511
Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance
Connell, S. R., Tracz, D. M., Nierhaus, K. H., & Taylor, D. E. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.12.3675-3681.2003 · Cited by 449
Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance
Hinrichs, W., Kisker, C., Düvel, M., Müller, A., Tovar, K., Hillen, W., & Saenger, W. (1994) · Science · doi:10.1126/science.8153629 · Cited by 408
The A-Z of bacterial translation inhibitors
Wilson, D. N. (2009) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409230903307311 · Cited by 322
Self-citationJenner, L., Starosta, A. L., Terry, D. S., Mikolajka, A., Filonava, L., Yusupov, M., Blanchard, S. C., Wilson, D. N., & Yusupova, G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216691110 · Cited by 204
Self-citationTarget- and resistance-based mechanistic studies with TP-434, a novel fluorocycline antibiotic
Grossman, T. H., Starosta, A. L., Fyfe, C., O'Brien, W., Rothstein, D. M., Mikolajka, A., Wilson, D. N., & Sutcliffe, J. A. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.06187-11 · Cited by 162
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Cited by
Bacterial Resistance to Antimicrobial Agents
Varela, M. F., Stephen, J., Lekshmi, M., Ojha, M., Wenzel, N., Sanford, L. M., Hernandez, A. J., Parvathi, A., & Kumar, S. H. (2021) · Antibiotics · doi:10.3390/antibiotics10050593 · Cited by 292
Staphylococcus aureus: A Review of the Pathogenesis and Virulence Mechanisms
Touaitia, R., Mairi, A., Ibrahim, N. A., Basher, N. S., Idres, T., & Touati, A. (2025) · Antibiotics · doi:10.3390/antibiotics14050470 · Cited by 273
The bacterial translation stress response.
Starosta, A. L., Lassak, J., Jung, K., & Wilson, D. N. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12083 · Cited by 210
Self-citationStructural conservation of antibiotic interaction with ribosomes
Paternoga, H., Crowe-McAuliffe, C., Bock, L. V., Koller, T. O., Morici, M., Beckert, B., Myasnikov, A. G., Grubmüller, H., Nováček, J., & Wilson, D. N. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01047-y · Cited by 94
Self-citationMycoplasmas and Their Antibiotic Resistance: The Problems and Prospects in Controlling Infections
Chernova, O. A., Medvedeva, E. S., Mouzykantov, A. A., Baranova, N. B., & Chernov, V. M. (2016) · Acta Naturae · doi:10.32607/20758251-2016-8-2-24-34 · Cited by 66
Metadata
- Authors
- Nguyen, F., Starosta, A. L., Arenz, S., Sohmen, D., Dönhöfer, A., & Wilson, D. N.
- Venue
- Biological Chemistry
- Publisher
- Walter de Gruyter GmbH
- Published
- 2014-02-05
- Volume
- 395
- Issue
- 5
- Pages
- 559-575
- ISSN
- 1431-6730 (ISSN-L)
- 1437-4315
- OpenAlex
- W2020591349
- Cited by
- 528
- References
- 19
- FWCI
- 7.91
- Type
- journal article
- Language
- en
- Open access
- closed
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- Nguyen, F., Starosta, A. L., Arenz, S., Sohmen, D., Dönhöfer, A., & Wilson, D. N. (2014). Tetracycline antibiotics and resistance mechanisms. Biological Chemistry. https://doi.org/10.1515/hsz-2013-0292
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