INOR 210 |
| Iron is required for virulence of all bacterial pathogens. Many of these pathogens rely on small-molecule chelators, called siderophores, to scavenge iron in mammalian hosts. In an immune response, the human protein siderocalin binds both apo and ferric siderophores in order to intercept delivery of iron to the bacteria and thereby impede its virulence. Research in this field has only begun reveal an elaborate antagonism that exists between the bacteria and the host over iron. For example, we have demonstrated that Bacillus anthracis, the anthrax pathogen, relies on petrobactin, an exotic 3,4-catecholate siderophore that is not recognized by siderocalin, in order to ensure its iron supply. Through thermodynamic studies and fluorescence binding assays, with both natural and synthetic siderophores, we have determined that while it may be detrimental the efficiency of the siderophore in iron sequestration, structural modification may be advantageous to siderocalin evasion.
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General Inorganic Chemistry
7:00 PM-10:00 PM, Sunday, August 19, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Inorganic Chemistry |