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Enterotoxin Collection

"Unveiling the Molecular World of Enterotoxin: Exploring Cholera Toxin and Escherichia coli Heat-Labile Enterotoxins" Enterotoxins

Background imageEnterotoxin Collection: Cholera toxin, molecular model

Cholera toxin, molecular model
Cholera toxin. Molecular model of the secondary structure of cholera enterotoxin (intestinal toxin). The molecule consists of two subunits, A (top) and B (bottom)

Background imageEnterotoxin Collection: Cholera toxin molecule F006 / 9546

Cholera toxin molecule F006 / 9546
Cholera toxin, molecular model. Cholera toxin is a protein complex secreted by the bacterium Vibrio cholerae, that causes the disease cholera

Background imageEnterotoxin Collection: Staphylococcal enterotoxin C2 molecule F006 / 9506

Staphylococcal enterotoxin C2 molecule F006 / 9506
Staphylococcal enterotoxin C2. Molecular model of the C2 enterotoxin from the bacterium Staphylococcus aureus

Background imageEnterotoxin Collection: Escherichia coli heat-labile enterotoxin F006 / 9410

Escherichia coli heat-labile enterotoxin F006 / 9410
Escherichia coli heat-labile enterotoxin, molecular model. This is one of several proteins produced by pathogenic E. coli bacteria in the intestines

Background imageEnterotoxin Collection: T-cell receptor bound to enterotoxin

T-cell receptor bound to enterotoxin, molecular model. The T cell receptor (TCR) is a protein complex found on the surface of a type of white blood cell called T lymphocytes (or T cells)

Background imageEnterotoxin Collection: Escherichia coli heat-labile enterotoxin C013 / 7180

Escherichia coli heat-labile enterotoxin C013 / 7180
Escherichia coli heat-labile enterotoxin, molecular model showing secondary structure. This is one of several proteins produced by pathogenic E. coli bacteria in the intestines

Background imageEnterotoxin Collection: E. coli culture

E. coli culture
MODEL RELEASED. E. coli culture. Microbiologist holding a petri dish containing a culture of Escherichia coli bacteria. E. coli bacteria are normal inhabitants of the gut

Background imageEnterotoxin Collection: E. coli food poisoning

E. coli food poisoning
MODEL RELEASED. E. coli food poisoning. Composite image of a microbiologist holding a petri dish containing a culture of Escherichia coli bacteria and a sandwich. E

Background imageEnterotoxin Collection: Campylobacter food poisoning

Campylobacter food poisoning
MODEL RELEASED. Campylobacter food poisoning. Composite image of a microbiologist holding a petri dish containing a culture of Campylobacter sp. bacteria and cooked chicken. Campylobacter sp

Background imageEnterotoxin Collection: Bacillus cereus food poisoning

Bacillus cereus food poisoning
MODEL RELEASED. Bacillus cereus food poisoning. Microbiologist holding a petri dish containing a culture of B. cereus bacteria in one hand and a sample of reheated rice in the other. B

Background imageEnterotoxin Collection: Bacillus cereus culture

Bacillus cereus culture
MODEL RELEASED. Bacillus cereus culture. Microbiologist holding a petri dish containing a culture of B. cereus bacteria. B

Background imageEnterotoxin Collection: Cholera toxin, artwork

Cholera toxin, artwork
Cholera toxin, molecular structure. Cholera is an infectious intestinal disease caused by this toxin produced by the Gram-negative bacterium Vibrio cholerae



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"Unveiling the Molecular World of Enterotoxin: Exploring Cholera Toxin and Escherichia coli Heat-Labile Enterotoxins" Enterotoxins, such as Cholera toxin and Escherichia coli heat-labile enterotoxins, are fascinating molecules that have garnered significant attention in the field of microbiology. These toxins play a crucial role in causing gastrointestinal diseases by targeting specific cells within our bodies. One remarkable example is the Cholera toxin molecule (F006/9546), which exhibits an intricate molecular model. Its structure reveals how this toxin binds to host cells, triggering severe diarrhea and dehydration characteristic of cholera infections. Similarly, Staphylococcal enterotoxin C2 molecule (F006/9506) showcases another captivating aspect of enterotoxins. This particular molecule has been extensively studied due to its association with food poisoning outbreaks caused by contaminated foods. Escherichia coli heat-labile enterotoxins also contribute significantly to gastrointestinal illnesses. The molecular models F006/9412 and F006/9410 provide insights into their mechanisms of action, highlighting their ability to disrupt cellular functions and induce intestinal distress. Moreover, T-cell receptors bound to enterotoxin exemplify the complex interaction between these toxins and our immune system. Understanding this interplay can aid in developing effective treatments or vaccines against these harmful pathogens. The recurring presence of Cholera toxin molecules underscores its significance as a major player among enterotoxic agents. Its repeated appearance emphasizes ongoing research efforts aimed at comprehending its structure-function relationship for therapeutic advancements. Lastly, Escherichia coli heat-labile enterotoxin C013/7180 stands out due to its unique characteristics that distinguish it from other variants within this family of toxins. Exploring the world of enterotoxins through molecular models like those mentioned above sheds light on their intricate nature and provides a foundation for further research.