ArticleAntimicrobial agents and chemotherapy2005
Channel formation by CarO, the carbapenem resistance-associated outer membrane protein of Acinetobacter baumannii.
Article in Antimicrobial agents and chemotherapy, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 120 citations in OpenAlex.
- Decoding the genome of Acinetobacter baumannii from a urinary tract infection case: A comprehensive analysis of resistance, virulence, and genetic mobility attributes.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- A genome-wide association study to identify the genetic loci underlying carbapenem resistance in Acinetobacter baumannii.BMC genomics · 2026Article
- Identification of multiple Acinetobacter baumannii protein antigens as targets for potential immunotherapies using a novel protein microarray screening approach.PLoS pathogens · 2026Article
- Breaking the outer membrane barrier: structure, targets, and antimicrobial strategies for Gram-negative bacteria.Frontiers in microbiology · 2026Review
- Identification, resistance mechanisms, and innovative therapeutic approaches againstFrontiers in microbiology · 2026Review
- Development and validation of an interpretable machine learning-based model for predicting carbapenem-resistantFrontiers in cellular and infection microbiology · 2026Article
- Review
- Distribution of antimicrobial resistance genes and virulence genes in different genotypes of Acinetobacter baumannii.BMC infectious diseases · 2025Article
- Acinetobacter phages use distinct strategies to breach the capsule barrier.PLoS pathogens · 2025Article
- Combating Multidrug-ResistantInfection and drug resistance · 2025Review
- Global analysis of the RNA-RNA interactome in Acinetobacter baumannii AB5075 uncovers a small regulatory RNA repressing the virulence-related outer membrane protein CarO.Nucleic acids research · 2024Article
- Outer Membrane Vesicles fromVaccines · 2023Review
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- Co-Existence of Carbapenemase-Encoding Genes in Acinetobacter baumannii from Cancer Patients.Infectious diseases and therapy · 2021Article
- Design of a Multi-epitope Vaccine AgainstInternational journal of peptide research and therapeutics · 2021Article
- Genotypic and Phenotypic Characterization of Novel Sequence Types of Carbapenem-ResistantFrontiers in microbiology · 2021Article
- Antibiotic Resistance Profiles, Molecular Mechanisms and Innovative Treatment Strategies ofMicroorganisms · 2020Review
- An Evaluation of BfmR-Regulated Antimicrobial Resistance in the Extensively Drug Resistant (XDR)Frontiers in microbiology · 2020Article
- The Outer Membrane Proteins OmpA, CarO, and OprD ofFrontiers in microbiology · 2020Review
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has been recently shown that resistance to both imipenem and meropenem in multidrug-resistant clinical strains of Acinetobacter baumannii is associated with the loss of a heat-modifiable 25/29-kDa outer membrane protein, called CarO. This study aimed to investigate the channel-forming properties of CarO. Mass spectrometry analyses of this protein band detected another 25-kDa protein (called Omp25), together with CarO. Both proteins presented similar physicochemical parameters (M(w) and pI). We overproduced and purified the two polypeptides as His-tagged recombinant proteins. Circular dichroism analyses demonstrated that the secondary structure of these proteins was mainly a beta-strand conformation with spectra typical of porins. We studied the channel-forming properties of proteins by reconstitution into artificial lipid bilayers. In these conditions, CarO induced ion channels with a conductance value of 110 pS in 1 M KCl, whereas the Omp25 protein did not form any channels, despite its suggested porin function. The pores formed by CarO showed a slight cationic selectivity and no voltage closure. No specific imipenem binding site was found in CarO, and this protein would rather form unspecific monomeric channels.
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