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    The DOE Science News Source is a Newswise initiative to promote research news from the Office of Science of the DOE to the public and news media.
    • 2015-06-18 08:05:00
    • Article ID: 635906

    Argonne, Brandeis University Researchers Examine Infectious Bacterium's Natural Defenses

    Dreaded bacterial-related diseases have killed untold numbers of humans over the centuries. Today, two million illnesses and nearly 23,000 deaths can be attributed to antibiotic-resistant bacteria throughout the United States, say the Centers for Disease Control and Prevention.

    In May, the World Health Assembly took steps to combat antibiotic-resistant bacteria by endorsing a global plan to “improve access to affordable vaccines and address over- and under-nutrition,” prompting member states to put plans into action addressing everything from awareness of bacterial resistance to investment in countering antimicrobial resistance.

    Antibiotics fight bacteria by targeting enzymes essential to the bacterium's survival, like those involved in rebuilding the bacterium’s cellular wall. With many deadly bacteria able to resist antibiotics, scientists must work to design new compounds that target important functions in the bacteria to stop them from multiplying.

    As a spinoff from their research aimed at fighting a specific parasite, researchers at the U.S. Department of Energy’s Argonne National Laboratory and Brandeis University may have found a way around an infectious bacterium’s natural defenses.

    Brandeis University researcher Lizbeth Hedstrom initially developed an antimicrobial compound to combat the single-celled parasite Cryptosporidium parvum. The parasite, which infects the small intestine, can cause severe diarrhea in humans who ingest contaminated water. Hedstrom and her team discovered that an enzyme inside this protozoan parasite is similar to a number of enzymes from infectious bacteria.

    "Cryptosporidium looks like it got its enzyme gene from a bacterium," Hedstrom said. "Once we knew that, we could make a good guess that bacterial enzymes should be also targeted by the compound we created."

    Knowing that both the parasite and a number of infectious bacteria share similar biological processes was the first step.

    Hedstrom and her team spent years unlocking Cryptosporidium’s structure, cellular processes and key functions. But to test the hypothesis that their antimicrobial compound would work as effectively on bacteria as it does on the parasite, they would have to know just as much about the pathogenic bacteria they wanted to test. So she turned to the University of Chicago’s Center for Structural Genomics of Infectious Diseases (CSGID), Argonne’s Advanced Protein Characterization Facility (APCF), and the Advanced Photon Source.

    “Not only can we produce, define and crystallize proteins, but we can also process thousands of samples very quickly,” said Argonne Distinguished Fellow, Computation Institute Senior Fellow and Structural Biology Center Director Andrzej Joachimiak. “With an automated system using robots and state-of-the-art data processing and control software, we can help researchers clone and purify genes quickly.”

    The CSGID researchers decided to delete one “weak” part of the two-part enzyme, and to their surprise, this made the enzyme much easier to crystallize.

    The CSGID and APCF helped Hedstrom quickly define 13 bacterial structures from four different human pathogens. In lab tests, three enzymes were blocked, but the enzyme from the severe diarrhea-causing Vibrio cholerae was unaffected by the compound. Still, images gathered while defining the structure of the bacterial enzyme showed the mechanism by which the enzyme forms and breaks bonds with molecules, and it did so in an unexpected way. This is a rare occurrence that now informs Hedstrom and her team as to the details of process and location of where to target her compound.

    “It is just like a key in a lock,” Joachimiak said. “Even though we were not able to inhibit Vibrio cholerae, we weren’t able to actually open the door, but now we know how the key we are using should fit the lock.”

    Hedstrom’s next challenge became finding inhibitors that could get into bacteria. Though enzyme targets are very similar, parasites and bacteria differ significantly in how drugs bind to and affect their enzymes. Hedstrom’s compounds are designed to diffuse across lipid membranes and into Cryptosporidium, and are therefore very “oily.” Unfortunately, bacteria do not take up oily compounds very well, so she needed to make changes to the compound in order to cross the cell wall and enter bacteria. The Argonne structures show exactly where the inhibitors can be modified in order to make sure they fit squarely into the target area without losing the ability to inhibit the function of the enzyme.

    Having passed this hurdle, Hedstrom is optimistic about the future of her research and the puzzles she has yet to unlock.

    “I am excited to say that we have completed the initial step, which is identifying the compounds,” said Hedstrom. “It has been a long process, and we haven’t got a drug yet, but we would not be nearly as far along without Andrzej and Argonne’s team.”

    This research was published as "A Novel Cofactor-binding Mode in Bacterial IMP Dehydrogenases Explains Inhibitor Selectivity" in the January issue of the Journal of Biological Chemistry.

    The Advanced Photon Source is a DOE Office of Science User Facility. The Structural Biology Center is also supported by the DOE Office of Science, while the Center for Structural Genomics of Infectious Diseases is supported under a National Institutes of Health Contract. Other contributors to this work include Magdalena Makowska-Grzyska, Youngchang Kim, Natalia Maltseva, Jerzy Osipiuk, Minyi Gu, Minjia Zhang, Kavitha Mandapati, Deviprasad R. Gollapalli and Suresh Kumar Gorla.

    Argonne National Laboratory seeks solutions to pressing national problems in science and technology. The nation's first national laboratory, Argonne conducts leading-edge basic and applied scientific research in virtually every scientific discipline. Argonne researchers work closely with researchers from hundreds of companies, universities, and federal, state and municipal agencies to help them solve their specific problems, advance America's scientific leadership and prepare the nation for a better future. With employees from more than 60 nations, Argonne is managed by UChicago Argonne, LLC for the U.S. Department of Energy's Office of Science. For more, visit www.anl.gov.

    DOE’s Office of Science is the single largest supporter of basic research in the physical sciences in the United States, and is working to address some of the most pressing challenges of our time. For more information, please visit science.energy.gov.

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    A Breakthrough in the Study of Laser/Plasma Interactions

    A Breakthrough in the Study of Laser/Plasma Interactions

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    Five new innovators join Chain Reaction Innovations in third cohort

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    Tim Knewitz named Argonne National Laboratory's Chief Financial Officer

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    Brookhaven Joins the IBM Q Network Hub at Oak Ridge National Lab

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    David Reis named head of PULSE Institute for ultrafast science

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    Long before David Reis joined the faculty of the Department of Energy's SLAC National Accelerator Laboratory and Stanford University, he was helping lay the groundwork for the lab's first-of-a-kind X-ray free-electron laser, or XFEL, and the revolutionary science that followed its opening in 2009. Now he's director of the PULSE Institute, which was founded by SLAC and Stanford with the express purpose of exploiting the possibilities for ultrafast science at that X-ray laser, the Linac Coherent Light Source (LCLS).

    Head of NSTX-U research is appointed deputy director for research at the Princeton Plasma Physics Laboratory

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    Argonne scientist advances energy sciences through professional leadership

    Argonne scientist advances energy sciences through professional leadership

    Ralph Muehleisen of the U.S. Department of Energy's (DOE) Argonne National Laboratory was recently re-elected to the Board of Directors of IBPSA-USA, the U.S. affiliate of the International Building Performance Simulation Association. IBPSA is a global leader in the promotion of building simulation science and one of the largest professional organizations in the world for building scientists and engineers.

    Brookhaven Lab Publishes Second Edition of Nuclear Nonproliferation Textbook

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    Capturing Energy Flow in a Plasma by Measuring Scattered Light

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    Artificial Intelligence and Deep Learning Accelerate Efforts to Develop Clean, Virtually Limitless Fusion Energy

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    Splitting Water Fast! Catalyst Works Faster than Mother Nature

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    The Weak Side of the Proton

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    A precision measurement of the proton's weak charge narrows the search for new physics.

    Fast-Moving Pairs May Solve 35-Year-Old Mystery

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    Physicists develop a universal mathematical description that suggests that proton-neutron pairs in a nucleus may explain why their associated quarks have lower average momenta than predicted.

    Team Takes Fluoride from Taps and Toothpaste to Batteries

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    With user facilities, researchers devise novel battery chemistries to help make fluoride batteries a reality.

    Quarks Under Pressure in the Proton

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    Magnetic Levitation of Ultracold Neutrons Yields New Measurement of the Neutron Lifetime

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    Storing extremely slow neutrons in a novel trap enables precise measurement of a basic property of particle physics.


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