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Fluorescein analogues inhibit SecA ATPase: the first sub-micromolar inhibitor of bacterial protein translocation.
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SecA is a central component of the general secretion system that is essential for bacterial growth and thus an ideal target for antimicrobial agents. A series of fluorescein analogues were first screened against the ATPase activity using the truncated unregulated SecA catalytic domain. Rose bengal (RB) and erythrosin B (EB) were found to be potent inhibitors SecA with IC 50 values of 0.5 μ M and 2 μ M, respectively. RB and EB inhibit the catalytic SecA ATPase more effectively than the F 1 F 0‐proton ATPase. We used three assays to test the effect of these compounds on full‐length SecA ATPase: in solution (intrinsic ATPase), in membrane preparation, and translocation ATPase. RB and EB show the following trend in terms of IC 50 values: translocation ATPase<membrane ATPase<intrinsic ATPase. Very importantly, the potency of these fluorescein analogues in inhibiting the truncated SecA ATPase correlates with their ability to inhibit the biologically relevant protein translocation activity of SecA. The in vitro translocation of proOmpA precursors into membrane vesicles is strongly inhibited by RB with IC 50 values of approximately 0.25 μ M, making RB the most potent inhibitor of SecA ATPase and SecA‐dependent protein translocation reported thus far. The ability of these compounds to inhibit SecA also directly translates into antibacterial effects. Our findings show the value of fluorescein analogues as probes for mechanistic studies of SecA functions and for the potential development of new antimicrobial agents with SecA as the target.
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4-oxo-5-cyano thiouracils, fluorescein analogs, and triazole-pyrimidine analogs are SecA inhibitors that are active against E. coli and S. aureus.
“Further studies identified 4-oxo-5-cyano thiouracils (Chaudhary et al., 2015), Fluorescein analogs (Huang et al., 2012) and triazole-pyrimidine analogs (Cui et al., 2016; Jin et al., 2016) as SecA inhibitors that are active against E. coli and S. aureus (Rao et al., 2014; De Waelheyns et al., 2015; Van Puyenbroeck and Vermeire, 2018).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Huang et al., 2012
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Cites
Comparison of simple potential functions for simulating liquid water
Jorgensen, W. L., Chandrasekhar, J., Madura, J., Impey, R., & Klein, M. (1983) · The Journal of Chemical Physics · doi:10.1063/1.445869 · Cited by 38,397
The Amber biomolecular simulation programs
Case, D. A., Cheatham, T. E., Darden, T., Gohlke, H., Luo, R., Merz, K. M., Onufriev, A., Simmerling, C., Wang, B., & Woods, R. J. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20290 · Cited by 9,535
Self-citationAn improved assay for nanomole amounts of inorganic phosphate
Lanzetta, P. A., Alvarez, L. J., Reinach, P. S., & Candia, O. A. (1979) · Analytical Biochemistry · doi:10.1016/0003-2697(79)90115-5 · Cited by 2,150
Casadaban, M. J. (1976) · Journal of Molecular Biology · doi:10.1016/0022-2836(76)90119-4 · Cited by 1,878
DOCK 4.0: Search strategies for automated molecular docking of flexible molecule databases
Ewing, T. J. A., Makino, S., Skillman, A. G., & Kuntz, I. D. (2001) · Journal of Computer-Aided Molecular Design · doi:10.1023/a:1011115820450 · Cited by 1,188
Protein Translocation Across the Bacterial Cytoplasmic Membrane
Driessen, A. J. M., & Nouwen, N. P. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061606.160747 · Cited by 635
Lill, R., Dowhan, W., & Wickner, W. (1990) · Cell · doi:10.1016/0092-8674(90)90742-w · Cited by 550
Development and validation of a modular, extensible docking program: DOCK 5
Moustakas, D. T., Lang, P. T., Pegg, S. C. ‐., Pettersen, E. F., Kuntz, I. D., Brooijmans, N., & Rizzo, R. C. (2006) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-006-9060-4 · Cited by 448
Oliver, D. B., Cabelli, R. J., Dolan, K. M., & Jarosik, G. P. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.21.8227 · Cited by 311
Ruiz, N., Falcone, B. V., Kahne, D. E., & Silhavy, T. J. (2005) · Cell · doi:10.1016/j.cell.2005.02.014 · Cited by 308
Bacterial protein secretion through the translocase nanomachine
Papanikou, E., Karamanou, S., & Economou, A. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1771 · Cited by 297
The Sec protein-translocation pathway
Mori, H., & Ito, K. (2001) · Trends in Microbiology · doi:10.1016/s0966-842x(01)02174-6 · Cited by 285
Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA
Hunt, J. F., Weinkauf, S., Henry, L., Fak, J. J., McNicholas, P. M., Oliver, D. B., & Deisenhofer, J. (2002) · Science · doi:10.1126/science.1074424 · Cited by 270
SecA protein is required for secretory protein translocation into E. coli membrane vesicles
Cabelli, R. J., Chen, L., Tai, P. C., & Oliver, D. B. (1988) · Cell · doi:10.1016/0092-8674(88)90227-9 · Cited by 236
Self-citationCabelli, R. J., Dolan, K. M., Qian, L. P., & Oliver, D. B. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54245-9 · Cited by 193
Foster, D. L., & Fillingame, R. H. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86880-1 · Cited by 182
Chemoablation of metastatic melanoma using intralesional Rose Bengal
Thompson, J. F., Hersey, P., & Wachter, E. A. (2008) · Melanoma Research · doi:10.1097/cmr.0b013e32831328c7 · Cited by 135
A molecular switch in SecA protein couples ATP hydrolysis to protein translocation
Spyridoula Karamanou, A., Vrontou, E., Sianidis, G., Baud, C., Roos, T., Kühn, A., Politou, A. S., & Economou, A. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01686.x · Cited by 129
Sianidis, G., Spyridoula Karamanou, A., Vrontou, E., Boulias, K., Repanas, K., Kyrpides, N. C., Politou, A. S., & Economou, A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.5.961 · Cited by 115
The cytotoxic and photodynamic inactivation of micro‐organisms by Rose Bengal
Banks, J. G., R.G. BOARD, Carter, J., & Dodge, A. D. (1985) · Journal of Applied Bacteriology · doi:10.1111/j.1365-2672.1985.tb01478.x · Cited by 87
A Significant Fraction of Functional SecA Is Permanently Embedded in the Membrane
Chen, X., Xu, H., & Tai, P. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.47.29698 · Cited by 83
Self-citationKnott, T. G., & Robinson, C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37125-9 · Cited by 76
Kanazawa, H., Miki, T., Tamura, F., Yura, T., & Futai, M. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.3.1126 · Cited by 70
CJ-21,058, a New SecA Inhibitor Isolated from a Fungus.
Sugie, Y., INAGAKI, S., Kato, Y., Nishida, H., PANG, C.-H., Saito, T., Sakemi, S., Dib-Hajj, F. B., Mueller, J. P., Sutcliffe, J. A., et al. (2002) · The Journal of Antibiotics · doi:10.7164/antibiotics.55.25 · Cited by 63
The first low μM SecA inhibitors
Chen, W., Huang, Y., Gundala, S. R., Yang, H., Li, M., Tai, P. C., & Wang, B. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.12.074 · Cited by 59
Self-citationDiscovery of the first SecA inhibitors using structure-based virtual screening
Li, M., Huang, Y., Tai, P. C., & Wang, B. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.01.135 · Cited by 56
Self-citationChen, X., Brown, T. M., & Tai, P. C. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.3.527-537.1998 · Cited by 55
Self-citationSynthesis of novel 5-amino-thiazolo[4,5-d]pyrimidines as E. coli and S. aureus SecA inhibitors
Jang, M., Jonghe, S. D., Segers, K., Anné, J., & Herdewijn, P. A. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.10.027 · Cited by 54
Signal Peptide Determinants of SecA Binding and Stimulation of ATPase Activity
Wang, L., Miller, A., & Kendall, D. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.14.10154 · Cited by 52
Jacobsverg, L., Kantrowitz, E. R., & Lipscomb, W. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40635-2 · Cited by 50
Li, M., & Wang, B. (2007) · Journal of Molecular Modeling · doi:10.1007/s00894-007-0245-0 · Cited by 49
Self-citationAntibacterial Compounds from Rose Bengal‐Sensitized Photooxidation of β‐Caryophyllene
Kim, Y. S., Park, S. J., Lee, E. J., Cerbo, R. M., Lee, S. M., Ryu, C.-H., Kim, G. S., Kim, J. O., & Ha, Y. L. (2008) · Journal of Food Science · doi:10.1111/j.1750-3841.2008.00879.x · Cited by 47
Parish, C. A., de la Cruz, M., Smith, S. K., Zink, D. L., Baxter, J., Tucker‐Samaras, S., Collado, J., Platas, G., Bills, G. F., Dı́ez, M. T., et al. (2008) · Journal of Natural Products · doi:10.1021/np800528a · Cited by 47
Zheng, S., Kaur, G., Wang, H., Li, M., Macnaughtan, M. A., Yang, X., Reid, S., Prestegard, J. H., Wang, B., & Ke, H. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm701635j · Cited by 44
Self-citationDiscovery of novel SecA inhibitors of Candidatus Liberibacter asiaticus by structure based design
Akula, N., Zheng, H., Han, F. Q., & Wang, N. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.05.086 · Cited by 41
Wang, H., Na, B., Yang, H., & Tai, P. C. (2007) · Journal of Bacteriology · doi:10.1128/jb.01633-07 · Cited by 41
Self-citationEscherichia coli SecA truncated at its termini is functional and dimeric
Spyridoula Karamanou, A., Sianidis, G., Gouridis, G., Pozidis, C., Papanikolau, Y., Papanikou, E., & Economou, A. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.01.025 · Cited by 40
Computational studies of H5N1 hemagglutinin binding with SA-α-2, 3-Gal and SA-α-2, 6-Gal
Li, M., & Wang, B. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.06.179 · Cited by 40
Self-citationRasooly, A., & Weisz, A. (2002) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.46.11.3650-3653.2002 · Cited by 40
Bacterial protein secretion — a target for new antibiotics?
Stephens, C. M., & Shapiro, L. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90217-9 · Cited by 38
Nakane, A., Takamatsu, H., Oguro, A., Sadaie, Y., Nakamura, K., & Yamane, K. (1995) · Microbiology · doi:10.1099/00221287-141-1-113 · Cited by 38
Foote, M. C., Burmeister, B. H., Thomas, J. M., & Smithers, B. M. (2010) · Melanoma Research · doi:10.1097/cmr.0b013e328331caa2 · Cited by 31
Morris, S. J., Silbergeld, E. K., Brown, R. R., & Haynes, D. H. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(82)91392-4 · Cited by 29
McNicholas, P. M., Rajapandi, T., & Oliver, D. B. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.24.7231-7237.1995 · Cited by 26
Chapter 3 Antimicrobial Properties of Hydroxyxanthenes
Waite-Cusic, J. G., & Yousef, A. E. (2009) · Advances in applied microbiology · doi:10.1016/s0065-2164(09)69003-1 · Cited by 23
Chapter 7 In Vitro Protein Translocation into Escherichia coli Inverted Membrane Vesicles
Tai, P. C., Tian, G., Xu, H., Lian, J. P., & Yu, J. N. (1991) · Methods in cell biology · doi:10.1016/s0091-679x(08)61680-5 · Cited by 21
Self-citationIn vitro protein translocation into Escherichia coli inverted membrane vesicles.
Tai, P. C., Tian, G., Xu, H., Lian, J. P., & Yu, J. N. (1991) · PubMed · Cited by 17
Self-citationSec, drugs and rock’n’roll: antibiotic targeting of bacterial protein translocation
Economou, A. (2001) · Emerging Therapeutic Targets · doi:10.1517/14728222.5.2.141 · Cited by 15
Interactions of erythrosin B (U.S. F, D & C Red 3) with rat cortical membranes
Silbergeld, E. K., Anderson, S. M., & Morris, S. J. (1982) · Life Sciences · doi:10.1016/0024-3205(82)90167-9 · Cited by 13
Watson, B. D., & Haynes, D. H. (1982) · Chemico-Biological Interactions · doi:10.1016/0009-2797(82)90108-9 · Cited by 13
Mignaco, J. A., Lupi, O. H., Santos, F. T., Barrabin, H., & Scofano, H. M. (1996) · Biochemistry · doi:10.1021/bi9518353 · Cited by 13
Interaction of tetraiodofluorescein with yeast hexokinase.
Yip, B. P., & Rudolph, F. B. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32956-3 · Cited by 12
Glaser, E. G., Cadenas, E., Andell, S., Ernster, L., Lönnberg, H., Berg, J.-E., Bartók, M., Pelczer, I., & Dombi, G. (1988) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.42b-0175 · Cited by 11
Fricke, U. (1985) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.1985.tb08865.x · Cited by 11
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Liao, Y., Kuo, S., Chiang, M., Lee, Y., Sung, W., Chen, Y.-H., Chen, T.-L., & Fung, C. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01343-15 · Cited by 67
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Metadata
- Authors
- Huang, Y., Wang, H., Gao, F., Li, M., Yang, H., Wang, B., & Tai, P. C.
- Affiliations
- Georgia State University (US)
- University of Massachusetts Chan Medical School (US)
- Shandong University (CN)
- Corresponding author
- Wang, Binghe
- Tai, Phang C.
- Venue
- ChemMedChem
- Publisher
- Wiley
- Published
- 2012-02-22
- Volume
- 7
- Issue
- 4
- Pages
- 571-577
- ISSN
- 1860-7179 (ISSN-L)
- 1860-7187
- PMC
- PMC3483595
- OpenAlex
- W2070724434
- Cited by
- 42
- References
- 54
- Citations by year
- 2025: 4 · 2024: 3 · 2023: 2 · 2022: 1 · 2021: 8 · 2020: 4 · 2018: 2 · 2017: 1 · 2016: 5 · 2015: 5 · 2014: 5 · 2013: 2
- FWCI
- 2.31
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- ChemMedChem (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM034766, GM 34766)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- SecA ATPase, rose bengal, erythrosin B, protein translocation, bacterial protein secretion, ATPase inhibitors, antibacterial agents
- MeSH terms
- SEC Translocation Channels, SecA Proteins, Adenosine Triphosphatases, Anti-Bacterial Agents, Bacillus subtilis, Bacterial Outer Membrane Proteins, Bacterial Proteins, Drug Evaluation, Preclinical, Enzyme Inhibitors, Erythrosine, Escherichia coli, Models, Molecular, Rose Bengal, Fluorescein, Inhibitory Concentration 50, Protein Transport, Membrane Transport Proteins
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 ›
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