ArticleProceedings of the National Academy of Sciences of the United States of America2013
Molecular basis of antibiotic multiresistance transfer in Staphylococcus aureus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
29 citing papers in PubMed, 49 citations in OpenAlex.
- Clinical Rel mutations that increase basal (p)ppGpp promote conjugal transfer of staphylococcal resistance plasmids.Microbiology (Reading, England) · 2026Article
- Type IV secretion systems: reconciling diversity through a unified nomenclature.FEMS microbiology reviews · 2026Review
- Predicting Single-Stranded DNA Oligonucleotides 3D Structures: An Open Issue.Computational and structural biotechnology journal · 2026Article
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- Structural and biochemical characterization of the relaxosome auxiliary proteins encoded on theComputational and structural biotechnology journal · 2022Article
- Molecular underpinnings of ssDNA specificity by Rep HUH-endonucleases and implications for HUH-tag multiplexing and engineering.Nucleic acids research · 2021Article
- DNA processing by the MOBH family relaxase TraI encoded within the gonococcal genetic island.Nucleic acids research · 2019Article
- Regulation of Gram-Positive Conjugation.Frontiers in microbiology · 2019Review
- Article
- Characterization of a relaxase belonging to the MOBMobile DNA · 2019Article
- Identification and characterization of a novel antimicrobial peptide compound produced bySaudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2018Article
- Staphylococcal Plasmids, Transposable and Integrative Elements.Microbiology spectrum · 2018Review
- Defining the binding determinants ofThe Journal of biological chemistry · 2018Article
- Structural basis of a histidine-DNA nicking/joining mechanism for gene transfer and promiscuous spread of antibiotic resistance.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Sequence-Directed Covalent Protein-DNA Linkages in a Single Step Using HUH-Tags.Journal of the American Chemical Society · 2017Article
- In vitro transfer of methicillin resistance determinants mecA from methicillin resistant Staphylococcus aureus (MRSA) to methicillin susceptible Staphylococcus aureus (MSSA).BMC microbiology · 2017Article
- Staphylococcus aureus lactate- and malate-quinone oxidoreductases contribute to nitric oxide resistance and virulence.Molecular microbiology · 2016Article
- Orthogonal Protein Assembly on DNA Nanostructures Using Relaxases.Angewandte Chemie (International ed. in English) · 2016Article
- Processing of Nonconjugative Resistance Plasmids by Conjugation Nicking Enzyme of Staphylococci.Journal of bacteriology · 2016Article
- Design of Novel Relaxase Substrates Based on Rolling Circle Replicases for Bioconjugation to DNA Nanostructures.PloS one · 2016Article
Corrections and comments
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Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
Abstract
Multidrug-resistant Staphylococcus aureus infections pose a significant threat to human health. Antibiotic resistance is most commonly propagated by conjugative plasmids like pLW1043, the first vancomycin-resistant S. aureus vector identified in humans. We present the molecular basis for resistance transmission by the nicking enzyme in S. aureus (NES), which is essential for conjugative transfer. NES initiates and terminates the transfer of plasmids that variously confer resistance to a range of drugs, including vancomycin, gentamicin, and mupirocin. The NES N-terminal relaxase-DNA complex crystal structure reveals unique protein-DNA contacts essential in vitro and for conjugation in S. aureus. Using this structural information, we designed a DNA minor groove-targeted polyamide that inhibits NES with low micromolar efficacy. The crystal structure of the 341-residue C-terminal region outlines a unique architecture; in vitro and cell-based studies further establish that it is essential for conjugation and regulates the activity of the N-terminal relaxase. This conclusion is supported by a small-angle X-ray scattering structure of a full-length, 665-residue NES-DNA complex. Together, these data reveal the structural basis for antibiotic multiresistance acquisition by S. aureus and suggest novel strategies for therapeutic intervention.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.