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Related Concept Videos

Bacterial Toxins01:12

Bacterial Toxins

49
Bacterial toxins are sophisticated virulence factors that enable pathogenic bacteria to interact with, invade, and damage host tissues. These toxins fall broadly into two types: protein exotoxins, which are secreted into the environment and target specific host receptors, and lipopolysaccharide endotoxins, which are structural components of the bacterial outer membrane released primarily during bacterial lysis or membrane shedding. Exotoxins generally act more selectively, binding to cell...
49
Types of Toxins01:36

Types of Toxins

4.0K
Humans continually engage with an environment rich in potentially harmful chemicals. These are introduced to our bodies through inhalation, ingestion, or skin contact. These chemicals exist in various forms, such as air and environmental pollutants, agricultural chemicals, organic solvents, and heavy metals.
Air pollutants, primarily gases, pose significant threats to respiratory health, leading to conditions like hypoxia, lung cancer, and in extreme cases, death.
Environmental pollutants like...
4.0K
Diphtheria01:28

Diphtheria

69
Diphtheria is an acute, toxin-mediated infectious disease that primarily affects the upper respiratory tract. It is caused by Corynebacterium diphtheriae, a Gram-positive, pleomorphic rod that lacks spore-forming capability and exhibits a characteristic club-shaped morphology under microscopic examination. While C. diphtheriae can asymptomatically colonize mucosal surfaces, clinical disease manifests only when the bacterial strain is lysogenized by a specific β-corynephage. This phage...
69
Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

945
Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin,...
945
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

4.0K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
4.0K
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

8.7K
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
8.7K

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Related Experiment Video

Updated: Mar 31, 2026

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
10:41

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance

Published on: January 3, 2012

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The structure of tagetitoxin.

Abil E Aliev1, Kersti Karu, Robin E Mitchell

  • 1Department of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, UK. A.E.Aliev@ucl.ac.uk.

Organic & Biomolecular Chemistry
|October 31, 2015
PubMed
Summary

The previously revised tagetitoxin structure is incorrect. New nuclear magnetic resonance (NMR) and mass spectrometry (MS) data support a revised tagetitoxin structure.

Area of Science:

  • Natural Products Chemistry
  • Structural Biology
  • Organic Chemistry

Background:

  • Tagetitoxin is a bacterial phytotoxin with potential applications in agriculture.
  • Previous structural revisions of tagetitoxin have been proposed based on limited data.

Purpose of the Study:

  • To re-evaluate and clarify the correct chemical structure of tagetitoxin.
  • To resolve discrepancies in the existing literature regarding tagetitoxin's molecular architecture.

Main Methods:

  • Detailed analysis of newly acquired Nuclear Magnetic Resonance (NMR) spectroscopy data.
  • Mass Spectrometry (MS) data analysis for molecular weight confirmation.

Main Results:

  • The previously revised structure of tagetitoxin was found to be inconsistent with the new NMR data.

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A High-throughput-compatible FRET-based Platform for Identification and Characterization of Botulinum Neurotoxin Light Chain Modulators
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Related Experiment Videos

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A High-throughput-compatible FRET-based Platform for Identification and Characterization of Botulinum Neurotoxin Light Chain Modulators
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  • A novel tagetitoxin structure is proposed that accurately fits both NMR and MS data.
  • Conclusions:

    • The proposed structure represents the most accurate elucidation of tagetitoxin to date.
    • This revised structure is crucial for understanding tagetitoxin's biological activity and for future synthetic efforts.