Scientists have determined a three-dimensional (3-D) molecular image of how anthrax toxin enters human cells, giving scientists more potential targets for blocking the toxin, the lethal part of anthrax bacteria. The finding also points to a possible way to design anthrax toxin molecules that selectively attack tumor cells, as described in the journal Nature published online July 4. The study, funded by the National Institute of Allergy and Infectious Diseases, part of the National Institutes of Health, was led by Robert C. Liddington, Ph.D., of the Burnham Institute in La Jolla, CA.
"This elegant work provides important new leads for the development of novel antitoxins to protect people from anthrax, a dangerous and serious bioterror threat," says NIAID Director Anthony S. Fauci, M.D. "It also leads us closer to therapies that could save lives late in the disease when large amounts of toxin are present and antibiotics are less effective."
Using an intense X-ray beam to determine the position of atoms in a crystal form of the protein complex, a scientific team mapped the 3-D structure of one of the anthrax toxins proteins docked to a human anthrax toxin receptor. Anthrax toxin uses a protein known as protective antigen to gain entry into human or animal cells. The protective antigen protein can bind either of two different cell receptors: CMG2 and TEM8. In this study, scientists solved the puzzle of the molecular structure of the protective antigen protein and CMG2 bound together.
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