IN THIS ISSUE .
August 19, 2009
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Under the microscope, an E. coli cell lights up like a fireball. Each bright dot marks a surface protein that tells the bacteria to move toward or away from nearby food and toxins. Using a new imaging technique, researchers can map the proteins one at a time and combine them into a single image. This lets them study patterns within and among protein clusters in bacterial cells, which don't have nuclei or organelles like plant and animal cells. Seeing how the proteins arrange themselves will help researchers better understand how cell signaling works. Courtesy of UC Berkeley biophysicists Derek Greenfield and Ann McEvoy.
The new H1N1 strain doesn't spread from person to person as easily as other types of flu. Now, a research team including MIT bioengineer Ram Sasisekharan has a better idea why. First, the team found that a protein on the surface of the virus can only bind weakly to receptors in our lungs. That means it takes a lot of virus particles—through extended close contact with an infected person—to effectively transmit. Second, this strain lacks a gene that helps flu viruses replicate rapidly. But don't relax just yet—the virus could mutate into a form that spreads more easily or resists current antiviral drugs and vaccines.
Anthrax bacteria can cause serious and even fatal infections, in part because they encase themselves in capsules that white blood cells can't detect. A protein on the bacteria's surface called CapD helps build this defense-dodging sheath. Thanks to an intense X-ray beam at Argonne National Laboratory, biophysicist Andrzej Joachimiak and colleagues have revealed this key protein's crystal structure. Now that they know how CapD is put together, they can look for ways to disrupt it so other drugs or our own immune systems can attack the bacteria.
Full story (Link no longer available)
Article abstract (from the June 16 online edition of the Journal of Biological Chemistry)
Rice University biochemist James McNew and colleagues have found that a protein called atlastin helps fuse together the endoplasmic reticulum (ER), dynamic meshworks of tubes that serve as protein factories in our cells. Studying fruit flies and human cell cultures, the researchers found that the ER broke apart with no atlastin, while extra atlastin built up the ER too much. In addition to revealing more about basic biology, the discovery could help scientists better understand some cases of the rare disease hereditary spastic paraplegia, where mutated atlastin disrupts ER structure and leads to partial paralysis.
Rather than studying individual objects acting alone, systems biologists piece together whole networks of proteins, genes or cell signals to understand what makes our bodies tick—or makes them sick. An interdisciplinary center led by Janet Oliver at the University of New Mexico combines experiments with computer modeling to study the real-time interactions between our innate and adaptive immune systems. The team of over 50 biologists, biophysicists, physicists, mathematicians, engineers and materials scientists—many of whom are women and minorities—could gain insights that lead to better treatments for asthma, allergies, inflammatory diseases and cancer.