Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Transduction

Transduction

Among the three main modes of HGT—transformation, conjugation, and transduction—transduction is unique in that it is mediated by bacteriophages, or bacterial viruses.Transduction occurs in two ways. Generalized transduction occurs during the lytic cycle of a bacteriophage infection. In this process, bacteriophages infect bacterial cells, replicate within them, and ultimately cause cell lysis, releasing newly assembled virions. Occasionally, random fragments of the bacterial genome...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Enhancing clinical utility of AI-based antimicrobial resistance models: a perspective.

mBio·2026

Same author

Standardized numbering and alignment of the KPC family of β-lactamases.

Antimicrobial agents and chemotherapy·2026

Same author

Resistance to novel β-lactam/β-lactamase inhibitors among carbapenem-resistant <i>Pseudomonas aeruginosa</i> and clinical implications in the prospective observational <i>Pseudomonas</i> study.

Antimicrobial agents and chemotherapy·2026

Same author

Sulbactam-durlobactam and cefiderocol combination treatment of <i>Burkholderia cenocepacia</i>-associated Fitz-Hugh-Curtis syndrome.

Antimicrobial agents and chemotherapy·2026

Same author

Role of Ambler Position 104 in Defining Substrate Specificity in the KPC Family of β-Lactamases.

ACS infectious diseases·2026

Same author

A Val292 substitution combined with an alanine duplication (ADUP) in the Ω loop of ADC β-lactamase confers reduced susceptibility to advanced β-lactam agents, including cefiderocol.

mBio·2026

Same journal

<i>In vitro</i> antibacterial activity of gepotidacin in combination with other antimicrobial agents against <i>Neisseria gonorrhoeae</i> isolates.

Antimicrobial agents and chemotherapy·2026

Same journal

Development of domain-specific probes of <i>Plasmodium falciparum</i> heat shock protein 70-1.

Antimicrobial agents and chemotherapy·2026

Same journal

Addressing therapeutic options for KPC-3-producing ST307-<i>Klebsiella pneumoniae</i>: insights from <i>in vitro</i> evolution and mutant prevention strategies.

Antimicrobial agents and chemotherapy·2026

Same journal

Indole-based hybrids target both asexual parasites and gametocytes of <i>Plasmodium falciparum</i> and synergize with lumefantrine.

Antimicrobial agents and chemotherapy·2026

Same journal

Lineage-specific loss of the type VI secretion system in <i>Acinetobacter baumannii</i> ST19 is associated with reduced accessory genome content.

Antimicrobial agents and chemotherapy·2026

Same journal

Genomic diversity and topical antimicrobial resistance in <i>Staphylococcus aureus</i> from clinical and carriage populations in the New York-New Jersey region.

Antimicrobial agents and chemotherapy·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jul 12, 2025

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

Published on: March 25, 2020

The directed evolution of NDM-1.

Caitlyn A Thomas¹, Zishuo Cheng¹, Christopher R Bethel²

¹Department of Chemistry and Biochemistry, Miami University , Oxford, Ohio, USA.

Antimicrobial Agents and Chemotherapy

|October 24, 2023

Summary

This summary is machine-generated.

New Delhi Metallo-β-lactamase (NDM-1) variants did not increase resistance to meropenem via amino acid changes. Increased transcription or altered zinc transport may be more critical for meropenem resistance in clinical settings.

Keywords:

NDM-1 antibiotic resistance antimicrobial resistance beta-lactamases beta-lactams drug resistance evolution

More Related Videos

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli

Published on: March 16, 2011

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

Related Experiment Videos

Last Updated: Jul 12, 2025

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

Published on: March 25, 2020

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli

Published on: March 16, 2011

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

Area of Science:

Microbiology
Enzymology
Drug Resistance

Background:

β-Lactam antibiotics are crucial therapeutics, but resistance is a growing concern.
β-Lactamases, particularly metallo-β-lactamases (MBLs), are key enzymes conferring resistance by hydrolyzing β-lactam bonds.
New Delhi Metallo-β-lactamase (NDM-1) is a clinically significant MBL requiring further study.

Purpose of the Study:

To investigate the in vitro protein evolution of NDM-1 β-lactamase.
To identify if amino acid substitutions in NDM-1 can enhance resistance to meropenem.

Main Methods:

Utilized error-prone polymerase chain reaction to generate NDM-1 variants.
Evaluated the resistance profiles of generated variants against meropenem.

Main Results:

No observed amino acid substitutions in NDM-1 variants conferred increased resistance to meropenem.
Protein evolution through amino acid changes does not appear to be a primary driver of meropenem resistance for NDM-1.

Conclusions:

Amino acid substitutions in NDM-1 are unlikely to be the main mechanism for increased meropenem resistance.
Alternative mechanisms, such as increased gene transcription or altered zinc ion transport, warrant further investigation for clinical relevance in NDM-1 mediated resistance.