SAN DIEGO, June 6 /PRNewswire/ -- Structural GenomiX (SGX) announced today that it has the published a scientific study in the June 6 issue of the peer-reviewed journal, Structure, that describes the structure and mechanism of action of LuxS, a critical enzyme involved in the virulence of many bacteria. LuxS proteins are part of the quorum-sensing pathway, which is a communication system that enables bacteria to respond collectively to challenges from the environment. Responses of this type, such as biofilm formation, contribute to resistance to antibiotics, so the study of these proteins could enable the discovery of new antibiotics.
The article describes how SGX has combined genomics and the company's high-throughput structure determination technology to determine the crystal structures of three LuxS orthologs (from different bacterial species). The parallel analysis of several related structures has been shown to be a powerful tool to understand the biochemical function and precise enzymatic mechanism of these proteins. Moreover, the researchers at SGX have identified the substrate-binding site, likely to be a promising target site against which to develop small molecules to inhibit the enzyme and treat bacterial infections. LuxS is part of SGX's unique bacterial structure database, 3D-ID(TM), to facilitate the discovery of a new generation of antibiotics to treat infectious disease.
``Our database of bacterial structures, which will be available shortly, includes important proteins coded for by essential bacterial genes representing potential drug targets,'' commented Dr. Tim Harris, President and CEO of SGX. ``We believe that this program will provide critical support to pharmaceutical companies working to find solutions to complex infectious diseases, and will strengthen SGX's position in the drug discovery arena.''
The issue of antibiotic resistance, and creating new drugs that avoid this problem, is a focus for the industry. According to SGX, the three-dimensional structural characterization of key bacterial proteins is extremely helpful for the discovery of drugs that are effective against infectious disease and that have minimal toxicity and reduced resistance. The company has assembled a team of structural biologists dedicated to characterizing bacterial protein structures and expects that the 3D-ID(TM) will become a key tool for pharmaceutical companies in their anti-bacterial lead discovery programs.
In recent years, the pharmaceutical and biotechnology industries engaged in the development of new antibiotics have faced the problem of bacterial resistance to antibiotics. This difficulty is becoming more worrying as an increasing number of antibiotics developed in the past are becoming ineffective owing to the resistance that bacteria develop against these drugs. The Institute of Medicine, a part of the National Academy of Sciences, has estimated that the annual cost of treating antibiotic resistant infections in the United States may be as high as $30 billion.
SGX is a pioneer in high-throughput protein structure determination. The company integrates advances in genomics, bioinformatics and X-ray crystallography into a high-throughput structure determination platform that transforms DNA sequence into three-dimensional protein structures. These structures reveal important functional and binding information that researchers can use to develop novel drugs. Protein structures determined by SGX will impact target validation and will enable efficient lead generation and optimization, currently a major industry bottleneck. SGX protein structures will be available to strategic partners across the biopharmaceutical, agricultural, and chemical industries. SGX recently acquired Prospect Genomics, Inc., and expanded its capabilities into computational chemistry and lead compound optimization. SGX currently employs over 100 people at its facilities in San Diego, CA, San Francisco, CA, and Argonne, Illinois. For more information, please see the company web site at stromix.com. |
