New UCLA research published in Nature may lead to an effective alternative to antibiotic drugs for treating bacterial diseases.
UCLA microbiologists report the discovery of a new class of genetic elements, similar to retroviruses, that operate in bacteria, allowing them to diversify their proteins to bind to a large variety of receptors. The team discovered this fundamental mechanism in the most abundant life?forms on Earth: bacteriophages, the viruses that infect bacteria.
"A problem with antibiotics is that bacteria can mutate and become resistant to a particular antibiotic, while the antibiotic is static and cannot change," said Jeffery F. Miller, professor and chair of microbiology, immunology and molecular genetics at UCLA, who holds UCLAs M. Philip Davis Chair in Microbiology and Immunology, and who led the research team. "Bacteriophages ("phages") are natures anti-microbials, and they are amazingly dynamic. If the bacterium mutates in an effort to evade, the bacteriophage can change its specificity using the mechanism we discovered, to kill the newly resistant bacterium."
Stuart Wolpert | EurekAlert!
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Scientists present work at prestigious SIGGRAPH conference
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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...
Scientists develop first tool to use machine learning methods to compute flow around interactively designable 3D objects. Tool will be presented at this year’s prestigious SIGGRAPH conference.
When engineers or designers want to test the aerodynamic properties of the newly designed shape of a car, airplane, or other object, they would normally model...
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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