Browse AMR Genes
Explore antimicrobial resistance genes from the literature
Explore antimicrobial resistance genes from the literature
outer membrane protease
Overview
| Allele | Database | Papers | Drug Classes | Organisms | Countries | Years | Sequence Accession | Protein Accession |
|---|---|---|---|---|---|---|---|---|
| ompT | Reslit | 9 | Polymyxin b, Aminoglycoside +1 | Escherichia coli +4 | Canada|USA, Northern Palestinian territories|Northern Palestine, China|USA | 2012, 2013, 2019, 2020, 2022, 2023, 2024, 2025 | PRJNA551561|PRJNA551565|PRJNA551566 | - |
| OmpT |
Reslit |
| 1 |
| - |
| E. coli |
| - |
| - |
| - |
| - |
| Vcho_OmpT | Card Database | 1 | - | Vibrio cholerae | - | - | AF079766.2 | AAC28105.1 |
OmpT outer membrane proteases of enterohemorrhagic and enteropathogenic Escherichia coli contribute differently to the degradation of human LL-37.
OmpT outer membrane protease of EHEC and EPEC contributes to the degradation of human LL-37 and synthetic α-helical peptide C18G, with EHEC OmpT showing greater efficiency in degradation compared to EPEC OmpT.
Role of the Vibrio cholerae matrix protein Bap1 in cross-resistance to antimicrobial peptides.
The study identifies Bap1 and OmpT as critical factors in Vibrio cholerae's cross-resistance to antimicrobial peptides Polymyxin B and LL-37. Bap1 binds to OmpT on outer membrane vesicles (OMVs) and traps LL-37, reducing its effectiveness. OmpT's LDV domain is essential for Bap1 binding.
Antimicrobial Peptides and Their Mechanisms of Action Against Pathogens
Identification and characterization of OmpT-like proteases in uropathogenic Escherichia coli clinical isolates.
The study identified and characterized OmpT and arlC, two OmpT-like proteases in uropathogenic E. coli (UPEC) clinical isolates, which cleave and inactivate antimicrobial peptides, contributing to antimicrobial resistance.
Outer Membrane Vesiculation Facilitates Surface Exchange and In Vivo Adaptation of Vibrio cholerae.
The study shows that hypervesiculation in Vibrio cholerae leads to faster adaptation to antimicrobial peptides and bile through the depletion of OmpT and accumulation of (di)glycine-modified lipid A, respectively.
Catestatin selects for colonization of antimicrobial-resistant gut bacterial communities.
Catestatin treatment promotes the abundance of bacteria harboring antimicrobial resistance genes eptA and ompT, which confer resistance to Catestatin through phosphoethanolamine modification and protease-mediated degradation, respectively.
Omptin Proteases of Enterobacterales Show Conserved Regulation by the PhoPQ Two-Component System but Exhibit Divergent Protection from Antimicrobial Host Peptides and Complement.
The study identifies that omptin proteases in Enterobacterales, including OmpT, OmpP, ArlC, and CroP, are regulated by the PhoPQ two-component system and provide varying levels of protection against antimicrobial host peptides and complement.
Multiple resistance factors collectively promote inoculum-dependent dynamic survival during antimicrobial peptide exposure in Enterobacter cloacae.
The study identifies PhoPQ, RcsB, and OmpT as critical factors contributing to cecropin B resistance in Enterobacter cloacae, highlighting their roles in outer membrane modifications, membrane stress response, and proteolytic cleavage, respectively.
Molecular characterization of avian pathogenic Escherichia coli isolates from broiler farms in Northern Palestinian territories.
The study identified several virulence genes, including iroN, hlyF, iutA, tsh, iss, ompT, papGI, papGII, papC, and cva/cvi, which were associated with antibiotic resistance in APEC isolates from broiler farms in Northern Palestine. These genes were found to be prevalent among the isolates and correlated with resistance to multiple antibiotics.
Convergence of plasmid-driven virulence and antibiotic resistance in Escherichia coli.
The study identifies mcr-1 as a key gene conferring colistin resistance in ColVLP co-integrates, highlighting the convergence of virulence and resistance on plasmids in E. coli.
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