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Related Concept Videos

Diphtheria01:28

Diphtheria

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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...
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Bacterial Toxins01:12

Bacterial Toxins

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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...
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Maturation of Endosomes01:28

Maturation of Endosomes

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The early endosome containing internalized molecules matures through transformations in its location, morphology, intraluminal pH, and membrane protein composition. Together, these changes result in a more acidic late endosome that contains multiple intraluminal vesicles; therefore, the late endosome is also called a multivesicular body (MVB).
Changes in location
The maturing endosome moves along microtubules from the periphery of the cell towards the perinuclear region. This movement of the...
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Receptor-mediated Endocytosis01:20

Receptor-mediated Endocytosis

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Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
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The Early Endosome: Endocytosis of Transferrin01:28

The Early Endosome: Endocytosis of Transferrin

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Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
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Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
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Related Experiment Video

Updated: Mar 30, 2026

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
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EFFECT OF DIPHTHERIA TOXIN T-DOMAIN ON ENDOSOMAL pH.

A J Labyntsev, N V Korotkevych, D V Kolybo

    Ukrainian Biochemical Journal
    |November 10, 2015
    PubMed
    Summary

    The diphtheria toxin's transport domain (Td) slows endosomal transport and prevents acidification. This mechanism may facilitate the catalytic domain's (Cd) entry into the cytosol for cytotoxic action.

    Area of Science:

    • Cell Biology
    • Molecular Biology
    • Toxicology

    Background:

    • Diphtheria toxin (DT) cytotoxicity involves transferring its catalytic domain (Cd) into the cytosol from endosomes.
    • The transport domain (Td) is crucial for this process, but its mechanism is unclear.
    • Previous work suggested Td influences DT's endosomal transport.

    Purpose of the Study:

    • To investigate how diphtheria toxin affects its own compartmentalization within the intracellular transport pathway.
    • To determine the impact of the transport domain (Td) on endosomal pH dynamics.
    • To elucidate the role of Td in the endosomal escape mechanism of DT.

    Main Methods:

    • Utilized recombinant diphtheria toxin (DT) fragments differing in Td presence, fused with fluorescent proteins.

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  • Tracked the intracellular transport pathway of DT fragments using colocalization with endosomal markers.
  • Monitored endosomal pH changes over time using fluorescence microscopy in live cells.

    • Main Results:

    • DT fragments with Td exhibited slower movement through the early-late endosome-lysosome pathway.
    • Colocalization patterns with endosomal markers differed between DT fragments with and without Td.
    • Endosomes containing Td-containing fragments maintained a stable pH (~6.5), while those without Td showed significant acidification (6.3 to 5.5).

    Conclusions:

    • The transport domain (Td) of diphtheria toxin inhibits endosomal acidification.
    • This pH-modulating property may involve Td forming an ion channel.
    • Inhibiting acidification and protease activation by Td likely promotes catalytic domain (Cd) translocation into the cytosol.