The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Daptomycin-Mediated Reorganization of Membrane Architecture Causes Mislocalization of Essential Cell Division Proteins
Open accessAbstract
Daptomycin is a lipopeptide antibiotic used clinically for the treatment of certain types of Gram-positive infections, including those caused by methicillin-resistant Staphylococcus aureus (MRSA). Details of the mechanism of action of daptomycin continue to be elucidated, particularly the question of whether daptomycin acts on the cell membrane, the cell wall, or both. Here, we use fluorescence microscopy to directly visualize the interaction of daptomycin with the model Gram-positive bacterium Bacillus subtilis. We show that the first observable cellular effects are the formation of membrane distortions (patches of membrane) that precede cell death by more than 30 min. Membrane patches are able to recruit the essential cell division protein DivIVA. Recruitment of DivIVA correlates with membrane defects and changes in cell morphology, suggesting a localized alteration in the activity of enzymes involved in cell wall synthesis that could account for previously described effects of daptomycin on cell wall morphology and septation. Membrane defects colocalize with fluorescently labeled daptomycin, DivIVA, and fluorescent reporters of peptidoglycan biogenesis (Bocillin FL and BODIPY FL-vancomycin), suggesting that daptomycin plays a direct role in these events. Our results support a mechanism for daptomycin with a primary effect on cell membranes that in turn redirects the localization of proteins involved in cell division and cell wall synthesis, causing dramatic cell wall and membrane defects, which may ultimately lead to a breach in the cell membrane and cell death. These results help resolve the longstanding questions regarding the mechanism of action of this important class of antibiotics.
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Of note, recent evidence suggests that DAP mainly targets the CM at the level of the division septum (86).”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [86]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“In addition, the stationary growth-phase conditions make it less likely that bacterial cell wall-active antibiotics (β-lactams and glycopeptides) are optimally effective.[77][78][79]”
From Infective Endocarditis in Adults: Diagnosis, Antimicrobial Therapy, and Management of Complications: A Scientific Statement for Healthcare Professionals From the American Heart Association (2015) · cites this paper as [78]
Experimental — accuracy not yet measured
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
Cites
Membrane curvature and mechanisms of dynamic cell membrane remodelling
McMahon, H. T., & Gallop, J. L. (2005) · Nature · doi:10.1038/nature04396 · Cited by 2,205
Control of Cell Morphogenesis in Bacteria
Daniel, R. A., & Errington, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00421-5 · Cited by 740
Regulation of endospore formation in Bacillus subtilis
Errington, J. (2003) · Nature Reviews Microbiology · doi:10.1038/nrmicro750 · Cited by 712
Correlation of Daptomycin Bactericidal Activity and Membrane Depolarization in Staphylococcus aureus
Silverman, J. A., Perlmutter, N. G., & Shapiro, H. M. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.8.2538-2544.2003 · Cited by 657
Self-citationBacterial viability and antibiotic susceptibility testing with SYTOX green nucleic acid stain
Roth, B. L., Poot, M., Yue, S. T., & Millard, P. J. (1997) · Applied and Environmental Microbiology · doi:10.1128/aem.63.6.2421-2431.1997 · Cited by 583
Membrane potential is important for bacterial cell division
Strahl, H., & Hamoen, L. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1005485107 · Cited by 572
Sterlini, J. M., & Mandelstam, J. (1969) · Biochemical Journal · doi:10.1042/bj1130029 · Cited by 559
Genetic Changes That Correlate with Reduced Susceptibility to Daptomycin in Staphylococcus aureus
Friedman, L., Alder, J. D., & Silverman, J. A. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00039-06 · Cited by 454
Self-citationStraus, S. K., & Hancock, R. E. W. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.02.009 · Cited by 446
Cui, L., Tominaga, E., Neoh, H., & Hiramatsu, K. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.50.3.1079-1082.2006 · Cited by 427
Research works printed but not linked: 1
- Ryter, 1965, Etude morphologie de la sporulation de Bacillus subtilis, Ann. Inst. Pasteur (Paris), 108, 40
Cited by
Sorted by citations
Items 101–200 of 319
Chow, H. Y., Po, K. H. L., Gao, P., Blasco, P., Wang, X., Li, C., Ye, L., Jin, K., Chen, K., Chan, E. W., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01957 · Cited by 53
Sabat, A. J., Tinelli, M., Grundmann, H., Akkerboom, V., Monaco, M., Grosso, M. D., Errico, G., Pantosti, A., & Friedrich, A. W. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02705 · Cited by 53
Daptomycin–Phosphatidylglycerol Domains in Lipid Membranes
Kreutzberger, M. A. B., Pokorny, A., & Almeida, P. F. F. (2017) · Langmuir · doi:10.1021/acs.langmuir.7b01841 · Cited by 52
Cell Envelope Stress Response in Cell Wall-Deficient L-Forms of Bacillus subtilis
Wolf, D., Domínguez‐Cuevas, P., Daniel, R. A., & Mascher, T. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00770-12 · Cited by 51
Cytological Profile of Antibacterial FtsZ Inhibitors and Synthetic Peptide MciZ
Araújo‐Bazán, L., Ruiz-Ávila, L. B., Andreu, D., Huecas, S., & Andreu, J. M. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.01558 · Cited by 50
Actinorhodin is a redox‐active antibiotic with a complex mode of action against G ram‐positive cells
Mak, S., & Nodwell, J. R. (2017) · Molecular Microbiology · doi:10.1111/mmi.13837 · Cited by 51
Govindarajan, S., Elisha, Y., Nevo‐Dinur, K., & Amster‐Choder, O. (2013) · mBio · doi:10.1128/mbio.00443-13 · Cited by 49
Molecular State of the Membrane-Active Antibiotic Daptomycin
Lee, M.-T., Hung, W.-C., Hsieh, M.-H., Chen, H., Chang, Y.-Y., & Huang, H. W. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.05.025 · Cited by 49
Harp, J. R., Saito, H. E., Bourdon, A. K., Reyes, J., Arias, C. A., Campagna, S. R., & Fozo, E. M. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.00933-16 · Cited by 48
Júnior, E. F. S., Menezes, L. F. S., de Araújo, I. F. S., & Schwartz, E. F. (2019) · Toxins · doi:10.3390/toxins11100563 · Cited by 46
Kotsogianni, I., Wood, T. M., Alexander, F. M., Cochrane, S. A., & Martin, N. I. (2021) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.1c00316 · Cited by 51
Revie, N. M., Iyer, K. R., Maxson, M. E., Zhang, J., Yan, S., Fernandes, C. M., Meyer, K. J., Chen, X., Skulska, I., Fogal, M., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31308-1 · Cited by 48
Wenzel, M., Dekker, M. P., Wang, B., Burggraaf, M. J., Bitter, W., van Weering, J. R. T., & Hamoen, L. W. (2021) · Communications Biology · doi:10.1038/s42003-021-01809-8 · Cited by 44
Next-Generation Phenotypic Screening
Warchal, S. J., Unciti‐Broceta, A., & Carragher, N. O. (2016) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0025 · Cited by 46
Analysis of Clostridium difficile biofilms: imaging and antimicrobial treatment
James, G. A., Chesnel, L., Boegli, L., Pulcini, E. D., Fisher, S. T., & Stewart, P. S. (2017) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkx353 · Cited by 46
Daptomycin Pore Formation and Stoichiometry Depend on Membrane Potential of Target Membrane
Seydlová, G., Sokol, A., Lišková, P., Konopásek, I., & Fišer, R. (2018) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01589-18 · Cited by 46
High-throughput reprogramming of an NRPS condensation domain
Folger, I. B., Frota, N., Pistofidis, A., Niquille, D. L., Hansen, D. A., Schmeing, T. M., & Hilvert, D. (2024) · Nature Chemical Biology · doi:10.1038/s41589-023-01532-x · Cited by 48
Alam, Z. A., Wu, X., Mascio, C. T. M., Chesnel, L., & Hurdle, J. G. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01087-15 · Cited by 45
Kebriaei, R., Rice, S., Singh, K. V., Stamper, K. C., Dinh, A. Q., Ríos, R., Díaz, L., Murray, B. E., Munita, J. M., Tran, T. T., et al. (2018) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00315-18 · Cited by 45
Environment Shapes the Accessible Daptomycin Resistance Mechanisms in Enterococcus faecium
Prater, A. G., Mehta, H. H., Kosgei, A. J., Miller, W. R., Tran, T. T., Arias, C. A., & Shamoo, Y. E. (2019) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00790-19 · Cited by 42
Müller, A., Grein, F., Otto, A., Gries, K., Orlov, D. S., Zarubaev, V. V., Girard, M., Sher, X., Валерьевна, Ш. О., Roemer, T., et al. (2017) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2017.12.002 · Cited by 46
Lee, C., Lee, J. H., Park, K. S., Jeong, B. C., & Lee, S. H. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00828 · Cited by 43
Zur Rolle der chemischen Synthese in der Entwicklung antibakterieller Wirkstoffe
Wright, P. M., Seiple, I. B., & Myers, A. G. (2014) · Angewandte Chemie · doi:10.1002/ange.201310843 · Cited by 43
Daptomycin for the treatment of bacteraemia due to vancomycin-resistant enterococci
Munita, J. M., Murray, B. E., & Arias, C. A. (2014) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2014.08.002 · Cited by 43
Antimicrobial natural products
Rahman, M. M., & Sarker, S. D. (2020) · Annual reports in medicinal chemistry · doi:10.1016/bs.armc.2020.06.001 · Cited by 43
Panesso, D., Reyes, J., Gaston, E. P., Deal, M., Londoño, A., Nigo, M., Munita, J. M., Miller, W. R., Shamoo, Y. E., Tran, T. T., et al. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01073-15 · Cited by 42
Baral, B., & Mozafari, M. R. (2020) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.0c00005 · Cited by 42
Antimicrobial Peptides: A Promising Solution to the Rising Threat of Antibiotic Resistance
Islam, T., Tamanna, N. T., Sagor, M. S., Zaki, R. M., Rabbee, M. F., & Lackner, M. K. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16121542 · Cited by 43
Arendt, W., Groenewold, M. K., Hebecker, S., Dickschat, J. S., & Moser, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.482935 · Cited by 41
Kleijn, L. H. J., Vlieg, H. C., Wood, T. M., Toraño, J. S., Janssen, B. J. C., & Martin, N. I. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201709240 · Cited by 40
Clinical Outcomes of Daptomycin for Vancomycin-resistant Enterococcus Bacteremia
Moise, P. A., Sakoulas, G., McKinnell, J. A., Lamp, K. C., DePestel, D. D., Yoon, M., Reyes, K., & Zervos, M. (2015) · Clinical Therapeutics · doi:10.1016/j.clinthera.2015.04.008 · Cited by 41
Stubbendieck, R. M., & Straight, P. D. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005807 · Cited by 8
Comparison of the Effects of Daptomycin on Bacterial and Model Membranes
Lee, M.-T., Yang, P.-Y., Charron, N. E., Hsieh, M.-H., Chang, Y.-Y., & Huang, H. W. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00818 · Cited by 38
Beriashvili, D., Taylor, R., Kralt, B., Mazen, N. A., Taylor, S. D., & Palmer, M. (2018) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2018.09.015 · Cited by 38
Fluorescent antibiotics for real-time tracking of pathogenic bacteria
Lu, M., Liu, W., Qiao, Q., Li, X., & Xu, Z. (2020) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2020.09.003 · Cited by 42
The Making and Taking of Lipids
Fozo, E. M., & Rucks, E. A. (2016) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2016.07.001 · Cited by 39
High-Dose Daptomycin and Clinical Applications
Jones, T. W., Jun, A. H., Michal, J. L., & Olney, W. J. (2021) · Annals of Pharmacotherapy · doi:10.1177/1060028021991943 · Cited by 37
Rajamuthiah, R., Jayamani, E., Conery, A. L., Fuchs, B. B., Kim, W., Johnston, T., Vilcinskas, A., Ausubel, F. M., & Mylonakis, E. E. (2015) · PLoS ONE · doi:10.1371/journal.pone.0128576 · Cited by 35
Kathayat, D., Helmy, Y. A., Deblais, L., & Rajashekara, G. (2018) · Scientific Reports · doi:10.1038/s41598-018-33587-5 · Cited by 34
Selbstorganisierte künstliche Ionenkanäle für die natürliche Selektion von Funktionen
Zheng, S., Huang, L., Sun, Z., & Barboiu, M. D. (2020) · Angewandte Chemie · doi:10.1002/ange.201915287 · Cited by 34
D’Angelo, K. A., Schissel, C. K., Pentelute, B. L., & Movassaghi, M. (2022) · Science · doi:10.1126/science.abm6509 · Cited by 34
Eradication of Staphylococcus aureus Biofilm Infection by Persister Drug Combination
Yee, R., Yuan, Y., Tarff, A., Brayton, C. F., Gour, N., Feng, J., & Zhang, Y. (2022) · Antibiotics · doi:10.3390/antibiotics11101278 · Cited by 32
Antimicrobial Peptides in Infectious Diseases and Beyond—A Narrative Review
Ιωάννου, Π., Baliou, S., & Kofteridis, D. P. (2023) · Life · doi:10.3390/life13081651 · Cited by 34
Chemoenzymatic synthesis of daptomycin analogs active against daptomycin-resistant strains
Scull, E. M., Bandari, C., Johnson, B. P., Gardner, E. D., Tonelli, M., You, J., Cichewicz, R. H., & Singh, S. (2020) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-020-10790-x · Cited by 31
On the quest for the elusive mechanism of action of daptomycin: Binding, fusion, and oligomerization
Zhang, J., Scott, W. R. P., Gabel, F., Wu, M., Desmond, R., Bae, J., Zaccaı̈, G., Algar, W. R., & Straus, S. K. (2017) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2017.07.020 · Cited by 30
The Antibiotic Peptide Daptomycin Functions by Reorganizing the Membrane
Pokorny, A., & Almeida, P. F. F. (2021) · The Journal of Membrane Biology · doi:10.1007/s00232-021-00175-0 · Cited by 30
High-Dose Daptomycin Therapy for Staphylococcal Endocarditis and When to Apply It
Smith, J. R., Claeys, K. C., Barber, K. E., & Rybak, M. J. (2014) · Current Infectious Disease Reports · doi:10.1007/s11908-014-0429-6 · Cited by 30
Prater, A. G., Mehta, H. H., Beabout, K., Supandy, A., Miller, W. R., Tran, T. T., Arias, C. A., & Shamoo, Y. E. (2021) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01317-20 · Cited by 27
Claeys, K. C., Fiorvento, A. D., & Rybak, M. J. (2014) · Infectious Diseases and Therapy · doi:10.1007/s40121-014-0051-9 · Cited by 29
Davlieva, M. G., Tovar-Yanez, A., DeBruler, K., Leonard, P. G., Zianni, M. R., Arias, C. A., & Shamoo, Y. E. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.09.016 · Cited by 30
Zhang, M., Zhu, P., Xin, P., Si, W., Li, Z., & Hou, J. (2017) · Angewandte Chemie · doi:10.1002/ange.201612093 · Cited by 28
Membrane rigidity regulates E. coli proliferation rates
Salinas-Almaguer, S., Mell, M., Almendro‐Vedia, V. G., Calero, M., Robledo-Sánchez, K. C. M., Ruiz-Suarez, C., Alarcón, T., Barrio, R. A., Hernández-Machado, A., & Monroy, F. (2022) · Scientific Reports · doi:10.1038/s41598-022-04970-0 · Cited by 27
Daptomycin Pore Formation Is Restricted by Lipid Acyl Chain Composition
Taylor, R., Beriashvili, D., Taylor, S. D., & Palmer, M. (2017) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.7b00138 · Cited by 26
Total Synthesis and Structural Establishment/Revision of Antibiotics A54145
Chen, D., Chow, H. Y., Po, K. H. L., Ma, W., Leung, E. L. Y., Sun, Z., Liu, M., Chen, S., & Li, X. (2019) · Organic Letters · doi:10.1021/acs.orglett.9b01972 · Cited by 26
Zhang, Y., Tan, X., Tu, X., Ling, F., & Wang, G. (2020) · Aquaculture · doi:10.1016/j.aquaculture.2020.735186 · Cited by 26
Rincón, S., Panesso, D., Díaz, L., Carvajal, L. P., Reyes, J., Munita, J. M., & Arias, C. A. (2014) · Biomédica · doi:10.7705/biomedica.v34i0.2210 · Cited by 39
Mycobacterial Membranes as Actionable Targets for Lipid-Centric Therapy in Tuberculosis
Modak, B., Girkar, S., Narayan, R., & Kapoor, S. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01870 · Cited by 26
Enterococcus faecalis and pathogenic streptococci inactivate daptomycin by releasing phospholipids
Ledger, E. V. K., Pader, V., & Edwards, A. M. (2017) · Microbiology · doi:10.1099/mic.0.000529 · Cited by 24
The Chiral Target of Daptomycin Is the 2 R ,2′ S Stereoisomer of Phosphatidylglycerol
Moreira, R., & Taylor, S. D. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202114858 · Cited by 24
Nature-inspired and medicinally relevant short peptides
Ciulla, M. G., Civera, M., Sattin, S., & Kumar, K. (2023) · Exploration of Drug Science · doi:10.37349/eds.2023.00011 · Cited by 26
Bacterial meningitis: new therapeutic approaches
Nau, R., Djukic, M., Spreer, A., & Eiffert, H. (2013) · Expert Review of Anti-infective Therapy · doi:10.1586/14787210.2013.839381 · Cited by 24
Adams, H. M., Li, X., Mascio, C. T. M., Chesnel, L., & Palmer, K. L. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00526-15 · Cited by 25
Reddy, P. J., Ray, S., Sathe, G. J., Prasad, T. S. K., Rapole, S., Panda, D., & Srivastava, S. (2015) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2014.0099 · Cited by 23
Mechanisms of Antibacterial Resistance
Oliveira, K. D. S., de Lima, L. A., Cobacho, N. B., Dias, S. C., & Franco, O. L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803642-6.00002-2 · Cited by 26
Hira, J., Uddin, M. J., Haugland, M. M., & Lentz, C. S. (2020) · Molecules · doi:10.3390/molecules25214949 · Cited by 23
Modes of Action of Antibacterial Agents
Allison, D., & Lambert, P. A. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397169-2.00032-9 · Cited by 23
Daptomycin Strongly Affects the Phase Behavior of Model Lipid Bilayers
Mescola, A., Ragazzini, G., & Alessandrini, A. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c06640 · Cited by 22
Modulation of Activity of Ultrashort Lipopeptides toward Negatively Charged Model Lipid Films
Wenda, J. M., Juhaniewicz, J., Tymecka, D., Konarzewska, D., & Sęk, S. (2017) · Langmuir · doi:10.1021/acs.langmuir.6b04674 · Cited by 21
Murray, B. E., Arias, C. A., & Nannini, E. C. (2015) · Elsevier eBooks · doi:10.1016/b978-1-4557-4801-3.00030-8 · Cited by 21
Smith, J. R., Yim, J., Rice, S., Stamper, K. C., Kebriaei, R., & Rybak, M. J. (2018) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00101-18 · Cited by 20
Ramos, Y., Sansone, S., Hwang, S., Sandoval, T. A., Zhu, M., Zhang, G., Cubillos‐Ruiz, J. R., & Morales, D. K. (2022) · mBio · doi:10.1128/mbio.02294-22 · Cited by 19
Growth Arrest of Staphylococcus aureus Induces Daptomycin Tolerance via Cell Wall Remodelling
Ledger, E. V. K., & Edwards, A. M. (2023) · mBio · doi:10.1128/mbio.03558-22 · Cited by 19
Yin, Y., Chen, H., Li, S., Gao, H., Sun, S., Li, H., Wang, R., Jin, L., Liu, Y., & Wang, H. (2019) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2019.08.021 · Cited by 19
Jusuf, S., Dong, P., Hui, J., Ulloa, E. R., Liu, G. Y., & Cheng, J. (2021) · Photochemistry and Photobiology · doi:10.1111/php.13389 · Cited by 18
Panda, G., Dash, S., & Sahu, S. K. (2022) · Membranes · doi:10.3390/membranes12100914 · Cited by 19
Molecular mechanisms of thioridazine resistance in Staphylococcus aureus
Wassmann, C. S., Lund, L. C., Thorsing, M., Lauritzen, S. P., Kolmos, H. J., Kallipolitis, B. H., & Klitgaard, J. K. (2018) · PLoS ONE · doi:10.1371/journal.pone.0201767 · Cited by 17
Jenson, R. E., Baines, S. L., Howden, B. P., Mishra, N. N., Farah, S., Lew, C. I., Berti, A. D., Shukla, S. K., Bayer, A. S., & Rose, W. E. (2020) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00890-20 · Cited by 18
Schäfer, A.-B., Sidarta, M., Nekhala, I. A., Righetto, G. M., Arshad, A., & Wenzel, M. (2024) · Microbiology Spectrum · doi:10.1128/spectrum.03275-23 · Cited by 18
Po, K. H. L., Chow, H. Y., Cheng, Q., Chan, B. K. W., Deng, X., Wang, S., Chan, E. W., Kong, H., Chan, K., Li, X., et al. (2021) · Natural Sciences · doi:10.1002/ntls.10023 · Cited by 17
Plasma Membrane-Cell Wall Feedback in Bacteria
García‐Heredia, A. (2023) · Journal of Bacteriology · doi:10.1128/jb.00433-22 · Cited by 17
Evolutionary history of Staphylococcus aureus influences antibiotic resistance evolution
Fait, A., Andersson, D. I., & Ingmer, H. (2023) · Current Biology · doi:10.1016/j.cub.2023.06.082 · Cited by 19
Modes of action of antibacterial agents
Allison, D., & Lambert, P. A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-818619-0.00133-7 · Cited by 17
Zeng, P., Wang, H., Zhang, P., & Leung, S. S. Y. (2024) · Biotechnology Advances · doi:10.1016/j.biotechadv.2024.108371 · Cited by 17
de Mello, S. S., Tyne, D. V., Lebreton, F., Silva, S. Q., Nogueira, M. C. L., Gilmore, M. S., & Camargo, I. L. B. D. C. (2019) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkz403 · Cited by 17
Fouad, A., Marzouk, A. A. E., Shaykoon, M. S. A., Ibrahim, S. M., El-Adl, S. M., & Ghanem, A. (2021) · Molecules · doi:10.3390/molecules26123527 · Cited by 17
Hurley, K. A., Heinrich, V. A., Hershfield, J. R., Demons, S. T., & Weibel, D. B. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00024 · Cited by 17
Taylor, S. D., & Moreira, R. (2024) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2024.04.003 · Cited by 16
Cockroaches, locusts, and envenomating arthropods: a promising source of antimicrobials.
Mosaheb, M. U. W. F. Z., Khan, N. A., & Siddiqui, R. (2018) · Europe PMC (PubMed Central) · doi:10.22038/ijbms.2018.30442.7339 · Cited by 16
Davlieva, M. G., Wu, C., Yue, Z., Arias, C. A., & Shamoo, Y. E. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b01072 · Cited by 15
[Resistance to "last resort" antibiotics in Gram-positive cocci: The post-vancomycin era].
Rincón, S., Panesso, D., Díaz, L., Carvajal, L. P., Reyes, J., Munita, J. M., & Arias, C. A. (2014) · PubMed · doi:10.1590/s0120-41572014000500022 · Cited by 16
Morris, M. A., Vallmitjana, A., Grein, F., Schneider, T., Arts, M., Jones, C. R., Nguyen, B. T., Hashemian, M. H., Malek, M., Gratton, E., et al. (2022) · Chemical Science · doi:10.1039/d2sc01388f · Cited by 15
Antimicrobial Peptides: The New Generation of Food Additives
Said, L. B., Fliss, I., Offret, C., & Beaulieu, L. (2018) · Elsevier eBooks · doi:10.1016/b978-0-08-100596-5.21718-6 · Cited by 15
Freeman, C. D., Hansen, T., Urbauer, R. J. B., Wilkinson, B. J., Singh, V. K., & Hines, K. M. (2024) · mSphere · doi:10.1128/msphere.00115-24 · Cited by 14
A Quantitative Model of Daptomycin Binding to Lipid Bilayers
Pokorny, A., Khatib, T. O., & Stevenson, H. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b07503 · Cited by 14
An atomic perspective on improving daptomycin's activity
Blasco, P., Zhang, C., Chow, H. Y., Chen, G., Yong-sheng, W., & Li, X. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.129918 · Cited by 14
Supandy, A., Mehta, H. H., Tran, T. T., Miller, W. R., Zhang, R., Xu, L., Arias, C. A., & Shamoo, Y. E. (2022) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02333-21 · Cited by 15
Tirilomis, T. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00097 · Cited by 14
McAuley, S., Huynh, A., Czarny, T. L., Brown, E. D., & Nodwell, J. R. (2018) · MedChemComm · doi:10.1039/c8md00009c · Cited by 14
Wüllner, D., Haupt, A., Prochnow, P., Leontiev, R., Slusarenko, A. J., & Bandow, J. E. (2019) · PROTEOMICS · doi:10.1002/pmic.201900064 · Cited by 14
Cafiso, V., Stracquadanio, S., Verde, F. L., Guidi, I. D., Zega, A., Pigola, G., & Stefani, S. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01893 · Cited by 14
Metadata
- Authors
- Pogliano, J., Pogliano, N., & Silverman, J. A.
- Affiliations
- University of California San Diego (US)
- Cubist Pharmaceuticals (United States) (US)
- ORCID
- Pogliano, J.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2012-06-01
- Volume
- 194
- Issue
- 17
- Pages
- 4494-4504
- ISSN
- 0021-9193 (ISSN-L)
- PMC
- PMC3415520
- OpenAlex
- W2113063737
- Cited by
- 319
- References
- 59
- Citations by year
- 2026: 8 · 2025: 10 · 2024: 23 · 2023: 19 · 2022: 23 · 2021: 22 · 2020: 27 · 2019: 27 · 2018: 23 · 2017: 30 · 2016: 30 · 2015: 29 · 2014: 25 · 2013: 18 · 2012: 5
- FWCI
- 14.84
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Journal of Bacteriology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM073898, GM073898)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Keywords
- daptomycin, antibiotic mechanism of action, membrane deformation, DivIVA, cell division proteins, cell wall biosynthesis, Bacillus subtilis, methicillin-resistant Staphylococcus aureus, cell morphology, septation
- MeSH terms
- Anti-Bacterial Agents, Bacillus subtilis, Bacterial Proteins, Cell Division, Cell Membrane, Cell Wall, Microbial Sensitivity Tests, Microscopy, Fluorescence, Peptidoglycan, Daptomycin, Cell Cycle 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 ›
Are you an author, or do you see a problem with this page? Request a review