ArticleAntimicrobial agents and chemotherapy2001
Mechanism of synergy between epigallocatechin gallate and beta-lactams against methicillin-resistant Staphylococcus aureus.
Article in Antimicrobial agents and chemotherapy, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.
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119 citing papers in PubMed, 385 citations in OpenAlex.
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- Beyond bactericidal: targeting plasmid-mediated antibiotic resistance with natural product-based plasmid curing agents.Frontiers in microbiology · 2026Review
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- Unveiling the Mechanisms of Bacterial Resistance and Countermeasures.Pathogens (Basel, Switzerland) · 2025Review
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- Flavonoids as Promising Natural Compounds for Combating Bacterial Infections.International journal of molecular sciences · 2025Review
- Evaluation of extracts from Phyllostachys makinoi for their antibacterial and accelerated wound healing potential.AMB Express · 2025Article
- Restoring Multidrug-ResistantAntibiotics (Basel, Switzerland) · 2024Article
- Green Tea Catechin Epigallocatechin Gallate Inhibits Vegetative Cell Outgrowth and Expression of Beta-Lactamase Genes in Penicillin-ResistantPathogens (Basel, Switzerland) · 2024Article
- Screening Tests for the Interaction ofAntibiotics (Basel, Switzerland) · 2024Article
- Phytotherapeutic potential against MRSA: mechanisms, synergy, and therapeutic prospects.Chinese medicine · 2024Article
- Enhanced Efficacy of Ciprofloxacin and Tobramycin againstAntibiotics (Basel, Switzerland) · 2024Article
59 more citing papers are in PubMed but not listed here.
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5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Compared to MICs (more than 800 microg/ml) of (-)-epigallocatechin gallate (EGCg) against Escherchia coli, MICs of EGCg against methicillin-susceptible and methicillin-resistant Staphylococcus aureus (MSSA and MRSA) were 100 microg/ml or less. Furthermore, less than 25 microg EGCg per ml obviously reversed the high level resistance of MRSA to all types of tested beta-lactams, including benzylpenicillin, oxacillin, methicillin, ampicillin, and cephalexin. EGCg also induced a supersusceptibility to beta-lactams in MSSA which does not express mecA, encoding penicillin-binding protein 2' (PBP2'). The fractional inhibitory concentration (FIC) indices of the tested beta-lactams against 25 isolates of MRSA were from 0.126 to 0.625 in combination with 6.25, 12.5 or 25 microg of EGCg per ml. However, no synergism was observed between EGCg and ampicillin against E. coli. EGCg largely reduced the tolerance of MRSA and MSSA to high ionic strength and low osmotic pressure in their external atmosphere, indicating damage of the cell wall. Unlike dextran and lipopolysaccharide, peptidoglycan from S. aureus blocked both the antibacterial activity of EGCg and the synergism between EGCg and oxacillin, suggesting a direct binding of EGCg with peptidoglycan on the cell wall. EGCg showed a synergistic effect with DL-cycloserine (an inhibitor of cell wall synthesis unrelated to PBP2') but additive or indifferent effect with inhibitors of protein and nuclear acid synthesis. EGCg did not suppress either PBP2' mRNA expression or PBP2' production, as confirmed by reverse transcription-PCR and a semiquantitative PBP2' latex agglutination assay, indicating an irrelevance between the synergy and PBP2' production. In summary, both EGCg and beta-lactams directly or indirectly attack the same site, peptidoglycan on the cell wall. EGCg synergizes the activity of beta-lactams against MRSA owing to interference with the integrity of the cell wall through direct binding to peptidoglycan.
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