ArticleAntimicrobial agents and chemotherapy2011
In vitro activities of arylomycin natural-product antibiotics against Staphylococcus epidermidis and other coagulase-negative staphylococci.
Article in Antimicrobial agents and chemotherapy, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 35 citations in OpenAlex.
- Fighting Antimicrobial Resistance: Innovative Drugs in Antibacterial Research.Angewandte Chemie (International ed. in English) · 2025Review
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- Inhibition of Protein Secretion inAntimicrobial agents and chemotherapy · 2019Article
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- The inhibition of type I bacterial signal peptidase: Biological consequences and therapeutic potential.Bioorganic & medicinal chemistry letters · 2015Review
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- Origins of Yersinia pestis sensitivity to the arylomycin antibiotics and the inhibition of type I signal peptidase.Antimicrobial agents and chemotherapy · 2015Article
- A putative cro-like repressor contributes to arylomycin resistance in Staphylococcus aureus.Antimicrobial agents and chemotherapy · 2015Article
- SecA: a potential antimicrobial target.Future medicinal chemistry · 2015Review
- Efforts toward broadening the spectrum of arylomycin antibiotic activity.Bioorganic & medicinal chemistry letters · 2013Article
- Mechanism of action of the arylomycin antibiotics and effects of signal peptidase I inhibition.Antimicrobial agents and chemotherapy · 2012Article
- Broadening the spectrum of β-lactam antibiotics through inhibition of signal peptidase type I.Antimicrobial agents and chemotherapy · 2012Article
- Harnessing the power of transposon mutagenesis for antibacterial target identification and evaluation.Mobile genetic elements · 2012Article
- Type I signal peptidase and protein secretion in Staphylococcus aureus.Journal of bacteriology · 2012Article
- Signal peptidase I: cleaving the way to mature proteins.Protein science : a publication of the Protein Society · 2012Review
- Imaging mass spectrometry and genome mining via short sequence tagging identified the anti-infective agent arylomycin in Streptomyces roseosporus.Journal of the American Chemical Society · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The arylomycins are a class of natural-product antibiotics that act via the inhibition of type I signal peptidase (SPase), and we have found in diverse bacteria that their activity is limited by the presence of a resistance-conferring Pro residue in SPase that reduces inhibitor binding. We have also demonstrated that Staphylococcus epidermidis, which lacks this Pro residue, is extremely susceptible to the arylomycins. Here, to further explore the potential utility of the arylomycins, we report an analysis of the activity of a synthetic arylomycin derivative, arylomycin C₁₆, against clinical isolates of S. epidermidis and other coagulase-negative staphylococci (CoNS) from distinct geographical locations. Against many important species of CoNS, including S. epidermidis, S. haemolyticus, S. lugdunensis, and S. hominis, we find that arylomycin C₁₆ exhibits activity equal to or greater than that of vancomycin, the antibiotic most commonly used to treat CoNS infections. While the susceptibility was generally correlated with the absence of the previously identified Pro residue, several cases were identified where additional factors also appear to contribute.
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