ArticleAntimicrobial agents and chemotherapy2014
Potential for reduction of streptogramin A resistance revealed by structural analysis of acetyltransferase VatA.
Article in Antimicrobial agents and chemotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
- Structure-based design and synthesis of group A streptogramins that bind to the nascent peptide exit tunnel of the ribosome.European journal of medicinal chemistry · 2026Article
- Biosynthesis and Synthesis of Griseoviridin and Viridogrisein.Synthesis · 2026Article
- Initial leads to combat streptogramin resistance generated from X-ray fragment screening against VatD.Structure (London, England : 1993) · 2025Article
- Genomic and Pathogenic Characterization of Vibrio alginolyticus CG-1 Isolated from Crassostrea gigas.Current microbiology · 2025Article
- Antechodynamics and Antechokinetics: Dynamics and Kinetics of Antibiotic Resistance Biomolecules.Biomolecules · 2025Review
- Mechanistic plasticity in ApmA enables aminoglycoside promiscuity for resistance.Nature chemical biology · 2024Article
- Hunted Wild Boars in Sardinia: Prevalence, Antimicrobial Resistance and Genomic Analysis ofFoods (Basel, Switzerland) · 2023Article
- Modular synthesis of streptogramin antibiotics.Synlett : accounts and rapid communications in synthetic organic chemistry · 2021Article
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- Modular synthesis enables molecular ju-jitsu in the fight against antibiotic resistance.Nature · 2020Article
- Freshwater viral metagenome reveals novel and functional phage-borne antibiotic resistance genes.Microbiome · 2020Article
- Structural and functional characterization of three Type B and C chloramphenicol acetyltransferases from Vibrio species.Protein science : a publication of the Protein Society · 2020Article
- Discovery of Furanoquinone Derivatives as a Novel Class of DNA Polymerase and Gyrase Inhibitors for MRSA Eradication in Cutaneous Infection.Frontiers in microbiology · 2019Article
- Genome sequence and comparative analysis of Bacillus cereus BC04, reveals genetic diversity and alterations for antimicrobial resistance.Functional & integrative genomics · 2018Article
- Phenotypic and molecular assessment of antimicrobial resistance profile of airborneAerobiologia · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
Combinations of group A and B streptogramins (i.e., dalfopristin and quinupristin) are "last-resort" antibiotics for the treatment of infections caused by Gram-positive pathogens, including methicillin-resistant Staphylococcus aureus and vancomycin-resistant Enterococcus faecium. Resistance to streptogramins has arisen via multiple mechanisms, including the deactivation of the group A component by the large family of virginiamycin O-acetyltransferase (Vat) enzymes. Despite the structural elucidation performed for the VatD acetyltransferase, which provided a general molecular framework for activity, a detailed characterization of the essential catalytic and antibiotic substrate-binding determinants in Vat enzymes is still lacking. We have determined the crystal structure of S. aureus VatA in apo, virginiamycin M1- and acetyl-coenzyme A (CoA)-bound forms and provide an extensive mutagenesis and functional analysis of the structural determinants required for catalysis and streptogramin A recognition. Based on an updated genomic survey across the Vat enzyme family, we identified key conserved residues critical for VatA activity that are not part of the O-acetylation catalytic apparatus. Exploiting such constraints of the Vat active site may lead to the development of streptogramin A compounds that evade inactivation by Vat enzymes while retaining binding to their ribosomal target.
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