For the first time, scientists have found that bacteria can use a Sonar-like system to spot other cells (either normal body cells or other bacteria) and target them for destruction. Reported in the December 24 issue of Science, this finding explains how some bacteria know when to produce a toxin that makes infection more severe. It may lead to the design of new toxin inhibitors. "Blocking or interfering with a bacteriums "detection" mechanism, should prevent toxin production and limit the severity of infection," says Michael Gilmore, PhD, lead author of the study, and currently director of research at the Schepens Eye Research Institute and professor of ophthalmology at Harvard Medical School.
Gilmore and his team have spent years studying the bacterium known as Enterococcus faecalis, one of the leading causes of hospital-acquired infections, to find new ways to treat them. These infections are frequently resistant to many, and sometimes all, antibiotics. Tens of thousands of deaths due to antibiotic resistant infection occur each year in the US, adding an estimated $ 4 Billion to health care costs. Scientist have known since 1934 that especially harmful strains of Enterococcus produce a toxin that destroys other cells, including human cells and even other types of bacteria. They also knew that this toxin was made only under some conditions. Until Gilmores study, scientists were unable to explain how the Enterococcus knew when to make it.
In the Science study, Gilmore and his team found that this toxin is made whenever there is another cell type in the environment near the bacterium, such as a human blood cell. They discovered how these bacteria know when other cells are present, and respond accordingly.
Patti Jacobs | EurekAlert!
Climate Impact Research in Hannover: Small Plants against Large Waves
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Scientists at the University of California, Los Angeles present new research on a curious cosmic phenomenon known as "whistlers" -- very low frequency packets...
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Researchers from TU Graz and their industry partners have unveiled a world first: the prototype of a robot-controlled, high-speed combined charging system (CCS) for electric vehicles that enables series charging of cars in various parking positions.
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
Actin is the most abundant protein in highly developed cells and has diverse functions in processes like cell stabilization, cell division and muscle...
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