Second Verse, Same as the First? Structures of Thioredoxin Proteins TrxA and TrxC from Mycobacterium tuberculosis (LB103)
Amari Junior, Brigitte Rios Llamosa, Anthony Richmond, Jhordy Rios Llamosa, Isioma Osademe, Michaun Cobb, Alexis S. Camacho, Jose Gonzalez Cruz, Carol Johnson, Terrence S. Neumann · The FASEB Journal · 2014
Mycobacterium tuberculosis , the causative agent for tuberculosis (TB), infected 8.6 million and killed 1.3 million people in 2012 (WHO). TB is most prevalent in countries with a high incidence of infectious diseases, such as HIV, due to weakened immune systems. TB mainly affects the lungs, but can also affect other systems. When a host organism is infected wtih TB, the Mycobacteria in the lungs multiply, often resulting in pneumonia, chest pain, and prolonged coughing. In response, host macrophages, a part of the natural immune system, engulf the Mycobacteria and oxidize bacterial cell proteins in an attempt to destroy it. To protect itself against this attack, the bacterial thioreductase system, consisting of the redox protein thioredoxin reductase (TrxR) and the thioredoxin proteins TrxA, TrxB, and TrxC, gives electrons back to the oxidized proteins. As this system works to maintain cellular redox homeostasis, finding ways to stop it might provide a new method for treating people with TB. TrxA and TrxC have similar structures, thus it can be hypothesized that their functions are similar. Comparing binding sites between the proteins can provide insight if TrxA can react with TrxR similarly to TrxC. By modeling TrxA and TrxC with 3D printing technology, the Messmer SMART Team (Students Modeling A Research Topic) can compare the structures of the thioredoxins which may lead to new strategies for curing or preventing TB. Grant Funding Source : Supported by a grant from NIH‐CTSA.