ArticleNature communications2022
Structural basis for PoxtA-mediated resistance to phenicol and oxazolidinone antibiotics.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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47 citing papers in PubMed, 70 citations in OpenAlex.
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- Characterization of a novel gene, Lsa(F), conferring resistance to pleuromutilins, lincosamides and streptogramin A in Streptococcus parasuis.Veterinary research · 2026Article
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- Structural insights into YheS-mediated release of SecM-arrested ribosome.Nature communications · 2026Article
- Multi-omic characterization of the sow colostrum and milk microbiome and proteome.Microbial genomics · 2026Article
- Emergence of Linezolid Resistance GenesInternational journal of molecular sciences · 2026Article
- The Alteromonas macleodii ribosome enables consecutive incorporation of bulky D-amino acids into peptides.Nucleic acids research · 2026Article
- Ribosomal protection as a linezolid resistance mechanism inAntimicrobial agents and chemotherapy · 2026Article
- A streamlined, nanopore-compatible 5PSeq protocol for rapid phenotypic antimicrobial sensitivity testing.Cell reports methods · 2026Article
- Global dissemination of optrA-mediated linezolid resistance in enterococci.The Journal of antimicrobial chemotherapy · 2026Article
- Environmental occurrence of optrA-mediated linezolid resistance in Enterococcus isolates and genomic insights into Enterococcus faecium ST54 co-harboring optrA, poxtA, and cfr(D) genes.World journal of microbiology & biotechnology · 2026Article
- Linezolid-resistant and vancomycin-resistantASM case reports · 2026Article
- Hybrid Antibiotics Targeting the Bacterial Ribosome.ACS central science · 2025Article
- Ribosomal protection as a linezolid resistance mechanism inbioRxiv : the preprint server for biology · 2025Article
- Therapeutic approach to difficult-to-treat multidrug-resistant enterococcal infections.Antimicrobial agents and chemotherapy · 2025Review
- Multifaceted roles of mycobacterial HflX: ribosome splitting, rRNA disordering, and drug resistance.Biochemical Society transactions · 2025Article
- ARTEM: a method for RNA and DNA tertiary motif identification with backbone permutations.Genome biology · 2025Article
Corrections and comments
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Authors and funding
13 authors at 8 institutions in 6 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PoxtA and OptrA are ATP binding cassette (ABC) proteins of the F subtype (ABCF). They confer resistance to oxazolidinone and phenicol antibiotics, such as linezolid and chloramphenicol, which stall translating ribosomes when certain amino acids are present at a defined position in the nascent polypeptide chain. These proteins are often encoded on mobile genetic elements, facilitating their rapid spread amongst Gram-positive bacteria, and are thought to confer resistance by binding to the ribosome and dislodging the bound antibiotic. However, the mechanistic basis of this resistance remains unclear. Here we refine the PoxtA spectrum of action, demonstrate alleviation of linezolid-induced context-dependent translational stalling, and present cryo-electron microscopy structures of PoxtA in complex with the Enterococcus faecalis 70S ribosome. PoxtA perturbs the CCA-end of the P-site tRNA, causing it to shift by ∼4 Å out of the ribosome, corresponding to a register shift of approximately one amino acid for an attached nascent polypeptide chain. We postulate that the perturbation of the P-site tRNA by PoxtA thereby alters the conformation of the attached nascent chain to disrupt the drug binding site.
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