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Related Concept Videos

Inhibitors of Bacterial Protein Synthesis01:25

Inhibitors of Bacterial Protein Synthesis

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Aminoglycosides constitute a highly potent class of bactericidal antibiotics that exert their antimicrobial effects by targeting the bacterial ribosome, specifically disrupting protein synthesis. These polycationic molecules consist of amino-modified sugars linked via glycosidic bonds to an aminocyclitol core such as 2-deoxystreptamine or streptamine. Their strong positive charges facilitate tight binding to the negatively charged phosphate backbone of ribosomal RNA (rRNA), primarily at the 16S...
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Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...
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Antimicrobial proteins are important components of the immune system. They aid the body in combating pathogens by either killing them directly or hindering their replication processes. Four main types of antimicrobial substances are interferons, the complement system, iron-binding proteins, and antimicrobial proteins.
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A Fluorescence-based Protocol for Preliminary Screening of Protein Synthesis Inhibitors from Natural Sources
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Natural Product-Derived Ianthelliformisamines Inhibit Protein Translation and Block Bacterial Flagellum Assembly.

Max Bottlinger1, Martino Morici2, Elena Fajardo-Ruiz3

  • 1Center for Functional Protein Assemblies, Department of Bioscience, TUM School of Natural Sciences, Technische Universität München, Ernst-Otto-Fischer-Straße 8, 85748 Garching, Germany.

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Ianthelliformisamines (Ian) show dual antibacterial and antivirulence effects against Gram-negative bacteria like E. coli. This study identified ribosomal protein biosynthesis initiation and flagellum assembly as key targets, offering new avenues for drug development.

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Area of Science:

  • Natural Product Chemistry
  • Microbiology
  • Chemical Biology

Background:

  • Ianthelliformisamines (Ian) are poorly characterized natural products with reported activity against Gram-negative bacteria.
  • The urgent need for new antibiotics necessitates exploring novel modes of action (MoA) from natural products.

Purpose of the Study:

  • To elucidate the mode of action of Ianthelliformisamines (Ian).
  • To synthesize Ian analogs and a chemical probe for activity-based protein profiling (ABPP).
  • To identify and validate cellular targets of Ian.

Main Methods:

  • Synthesis of Ian analogs and a chemical probe.
  • Activity-based protein profiling (ABPP) using the chemical probe.
  • Bacterial translation assays, motility assays, and transmission electron microscopy.
  • Invasion assays using pathogenic E. coli and human host cells.

Main Results:

  • Ian analogs retained antibacterial effects, enhanced by bicarbonate.
  • ABPP identified InfA (ribosomal protein biosynthesis initiation) and FliC (flagellum assembly) as targets.
  • Impaired bacterial motility and flagellum assembly were observed.
  • Ian treatment reduced the invasion of pathogenic E. coli into human host cells.

Conclusions:

  • Ianthelliformisamines (Ian) possess a dual antibacterial and antivirulence profile.
  • InfA and FliC are identified as key targets, revealing novel MoAs.
  • Activity-based chemical proteomics is effective in uncovering new targets for natural products, supporting therapeutic development.