Recently, scientists from the Seattle group, which includes Emerald BioStructures, the University of Washington and Pacific Northwest National Laboratory in addition to Seattle BioMed, provided structural data that offered insight into how specific differences in one of the RNA polymerase proteins in the swine flu virus changed the way it interacts with host cells, allowing it to infect humans. This information could provide a basis for future antiviral agents that could be used to prevent replication of the flu virus.
Other structures solved come from little known or emerging pathogens that cause disease and death, but have been less well studied by the research community. For example, the SSGCID solved the first protein structure from Rickettsia, bacterial pathogens carried by many ticks, fleas and lice that causes several forms of typhus and spotted fever.
Recently, scientists at CSGID determined the structure of a crucial enzyme in the shikimate pathway of Clostridium difficile, which is the most serious cause of antibiotic-associated diarrhea in humans and can lead to pseudomembranous colitis, a severe infection of the colon often resulting from eradication of the normal gut flora by antibiotics. The shikimate pathway is essential for plants and bacteria like C. difficile, but is not present in animals, making this enzyme an attractive antibiotic target. CSGID researchers have also determined the structures of numerous proteins from other disease-causing organisms such as Bacillus anthracis (anthrax), Salmonella enterica (salmonellosis food poisoning), Vibrio cholerae (cholera), Yersinia pestis (plague), and Staphylococcus aureus (staph infections).
The CSGID is a consortium which includes researchers from the University of Chicago (Chicago, IL), the J. Craig Venter Institute (Rockville, MD), University College London (London, United Kingdom), the University of Toronto (Toronto, Canada), the University of Virginia (Charlottesvill
|Contact: Erin White|