Getting “Rit‐R” Iron in the Cell: The Role of RitR in Reducing Iron Transport into Streptococcus pneumoniae. (LB111)

• Published in: The FASEB journal 2014-04, Vol.28 (S1), p.n/a
• Main Authors: Allbee, B., Anderson, N., Blank, D., Bolgert, J., Bothe, A., Britt, N., Geiser, E., Hammer, T., Janecek, E., Kalmer, I., Lawniczak, J., Lesiecki, M., Levy, J., Marshall, M., Meaux, N., Ruzicka, M., Temmer, J., Tiffany, K., Butt, A., Dyke, S., Vandenberg, B., Wankowski, J., Zeitlow, E., Tiffany, Karen, Silvaggi, Nicholas
• Format: Article
• Language: English
• ISSN: 0892-6638; 1530-6860
• DOI: 10.1096/fasebj.28.1_supplement.lb111

According to the World Health Organization, pneumonia is the leading cause of death in children worldwide, and infection of lung tissue by Streptococcus pneumonia causes the bulk of bacterial pneumonia cases in children. The atypical response regulator, RitR (Repressor of iron transport Regulator), helps S. pneumoniae survive in the hostile oxidizing conditions in the lungs. RitR has two domains, a DNA‐binding domain (DBD) and an aspartate‐less receiver domain (REC). In its “inactive” form, these domains are docked (i.e., close together) and the DBD is unable to bind DNA. In its “active” form, the domains are undocked; the DBD is freed from the REC. The “active” form dimerizes and can bind to DNA to turn off the iron transport genes. To study the changes that occur when RitR is activated, the Cedarburg High School SMART (Students Modeling A Research Topic) Team used 3D printing technology to model inactive RitR and a hypothetical active RitR dimer. RitR helps the bacterium survive in the oxygen‐rich environment in lungs by stopping iron transport into the bacterial cell. If iron is transported into the cell, oxygen forms reactive oxygen species that damage and kill cells. S. pneumonia cells without RitR are unable to infect lung tissue, so RitR is a potential target for drug design. Grant Funding Source: Supported by a grant from NIH‐CTSA.