Pore protein from staphylococcus aureus C013 / 9377
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Pore protein from staphylococcus aureus C013 / 9377
Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Computer artwork of the ribbon structure of the pore forming-toxin from the bacteria Staphylococcus aureus. The toxin targets white blood cells, part of the bodys immune system. It makes pores in the white blood cells membrane, causing the cell contents to leak, and thus killing the cell. This destruction of cells leads to skin and soft tissue infections. These are mainly abscesses, but it can also cause pneumonia. The toxin has been found in strains of the antibiotic-resistant MRSA (methicillin-resistant S. Aureus) bacteria
Science Photo Library features Science and Medical images including photos and illustrations
Media ID 9201083
© PASIEKA/SCIENCE PHOTO LIBRARY
Bacteria Bacterial Bonding Data Folding Hydrogen Lipid Membrane Models Mrsa Pore Proteins Resistant Ribbon Secondary Staphylococcus Staphylococcus Aureus Toxin Toxins Aureus Molecular Protein
EDITORS COMMENTS
This print showcases the intricate structure of staphylococcal alpha-hemolysin, a pore-forming toxin derived from the bacteria Staphylococcus aureus. The computer-generated artwork depicts the ribbon-like conformation of this protein, which plays a crucial role in causing skin and soft tissue infections. Staphylococcal alpha-hemolysin is notorious for its ability to target white blood cells, vital components of our immune system. By creating pores in the membrane of these cells, it triggers leakage of their contents and ultimately leads to cell death. This destructive mechanism not only results in abscesses but can also cause pneumonia. Of particular concern is that this toxin has been identified in strains of methicillin-resistant S. aureus (MRSA), a type of antibiotic-resistant bacteria. MRSA poses significant challenges in healthcare settings as it limits treatment options and increases the risk of severe infections. The image highlights various aspects critical to understanding this pore-forming toxin's function, including its secondary folding patterns and molecular interactions such as hydrogen bonding within lipid bilayers. These structural insights are invaluable for researchers studying potential therapeutic interventions against MRSA infections. Displayed by PASIEKA/SCIENCE PHOTO LIBRARY, this visually striking print serves as a reminder of both the beauty and complexity found within bacterial proteins while underscoring the urgent need for continued scientific exploration to combat antibiotic resistance effectively.
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