ArticleAntimicrobial agents and chemotherapy2016
Experimental Induction of Bacterial Resistance to the Antimicrobial Peptide Tachyplesin I and Investigation of the Resistance Mechanisms.
Article in Antimicrobial agents and chemotherapy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 72 citations in OpenAlex.
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- Marine Antimicrobial Peptides: Advances in Discovery, Multifunctional Mechanisms, and Therapeutic Translation Challenges.Marine drugs · 2025Review
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- Heterogeneous efflux pump expression underpins phenotypic resistance to antimicrobial peptides.eLife · 2025Article
- The Study of Antistaphylococcal Potential of Omiganan and Retro-Omiganan Under Flow Conditions.Probiotics and antimicrobial proteins · 2025Article
- Microwave-Assisted Synthesized ZnO@APTES Quantum Dots Exhibits Potent Antibacterial Efficacy Against Methicillin-ResistantInternational journal of nanomedicine · 2025Article
- The evolution of antimicrobial peptide resistance in Pseudomonas aeruginosa is severely constrained by random peptide mixtures.PLoS biology · 2024Article
- Mechanistic Study of Antimicrobial Effectiveness of Cyclic Amphipathic Peptide [RAntibiotics (Basel, Switzerland) · 2024Article
- Host Defense Proteins and Peptides with Lipopolysaccharide-Binding Activity from Marine Invertebrates and Their Therapeutic Potential in Gram-Negative Sepsis.Marine drugs · 2023Review
- Antimicrobial Activity and Immunomodulatory Properties of Acidocin A, the Pediocin-like Bacteriocin with the Non-Canonical Structure.Membranes · 2022Article
- Activity and Synergy of Cu-ATCUN Antimicrobial Peptides.International journal of molecular sciences · 2022Article
- Innate Immunity Mechanisms in Marine Multicellular Organisms.Marine drugs · 2022Review
- Identification of Antibacterial Peptide Candidates Encrypted in Stress-Related and MetabolicPharmaceuticals (Basel, Switzerland) · 2022Article
- Investigation of drug resistance of caries-related streptococci to antimicrobial peptide GH12.Frontiers in cellular and infection microbiology · 2022Article
- Co-expression Mechanism Analysis of Different Tachyplesin I-Resistant Strains inFrontiers in microbiology · 2022Article
- Molecular and Functional Analyses of the Primordial Costimulatory Molecule CD80/86 and Its Receptors CD28 and CD152 (CTLA-4) in a Teleost Fish.Frontiers in immunology · 2022Article
- The TonB system in Aeromonas hydrophila NJ-35 is essential for MacAVeterinary research · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tachyplesin I is a 17-amino-acid cationic antimicrobial peptide (AMP) with a typical cyclic antiparallel β-sheet structure that is a promising therapeutic for infections, tumors, and viruses. To date, no bacterial resistance to tachyplesin I has been reported. To explore the safety of tachyplesin I as an antibacterial drug for wide clinical application, we experimentally induced bacterial resistance to tachyplesin I by using two selection procedures and studied the preliminary resistance mechanisms. Aeromonas hydrophila XS91-4-1, Pseudomonas aeruginosa CGMCC1.2620, and Escherichia coli ATCC 25922 and F41 showed resistance to tachyplesin I under long-term selection pressure with continuously increasing concentrations of tachyplesin I. In addition, P. aeruginosa and E. coli exhibited resistance to tachyplesin I under UV mutagenesis selection conditions. Cell growth and colony morphology were slightly different between control strains and strains with induced resistance. Cross-resistance to tachyplesin I and antimicrobial agents (cefoperazone and amikacin) or other AMPs (pexiganan, tachyplesin III, and polyphemusin I) was observed in some resistant mutants. Previous studies showed that extracellular protease-mediated degradation of AMPs induced bacterial resistance to AMPs. Our results indicated that the resistance mechanism of P. aeruginosa was not entirely dependent on extracellular proteolytic degradation of tachyplesin I; however, tachyplesin I could induce increased proteolytic activity in P. aeruginosa Most importantly, our findings raise serious concerns about the long-term risks associated with the development and clinical use of tachyplesin I.
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