Re: Applied evolution

From: Dawsonzhu@aol.com
Date: Wed Nov 07 2001 - 08:50:08 EST

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    Marcio Pie wrote:

    > This paper just came out in the Annual Review of Ecology and Systematics.
    > This might answer Moorad's question a couple of weeks ago on practical
    > applications of evolutionary theory.
    >

    I just recently read an article in Nature Structural
    Biology (March 2001) related to this topic. In fact,
    if you use a search engine like

    http://www3.ncbi.nlm.nih.gov/entrez/query.fcgi

    you will about 1380 hits related to the keywords
    "drug resistance AND evolution"

    By Grace we proceed,
    Wayne
    ------------------------------------------------------
    Nat Struct Biol 2001 Mar;8(3):238-42
    Predicting the emergence of antibiotic resistance by
    directed evolution and structural analysis.

    Orencia MC, Yoon JS, Ness JE, Stemmer WP, Stevens RC.

    Department of Molecular Biology, The Scripps Research
    Institute, La Jolla, California 92037, USA.

    Directed evolution can be a powerful tool to predict
    antibiotic resistance. Resistance involves the accumulation
    of mutations beneficial to the pathogen while maintaining
    residue interactions and core packing that are critical for
    preserving function. The constraint of maintaining stability,
    while increasing activity, drastically reduces the number of
    possible mutational combination pathways. To test this theory,
    TEM-1 beta-lactamase was evolved using a hypermutator E.
    coli-based directed evolution technique with cefotaxime selection.
    The selected mutants were compared to two previous directed
    evolution studies and a database of clinical isolates. In
    all cases, evolution resulted in the generation of the
    E104K/M182T/G238S combination of mutations ( approximately
    500-fold increased resistance), which is equivalent to clinical
    isolate TEM-52. The structure of TEM-52 was determined to 2.4 A.
    G238S widens access to the active site by 2.8 A whereas E104K
    stabilizes the reorganized topology. The M182T mutation is
    located 17 A from the active site and appears to be a global
    suppressor mutation that acts to stabilize the new enzyme
    structure. Our results demonstrate that directed evolution
    coupled with structural analysis can be used to predict future
    mutations that lead to increased antibiotic resistance.



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