Tuberculosis is an ancient disease, signs of it were examined in Egyptian mummies. It is caused by the bacterium and pathogen, Mycobacterium tuberculosis, which infects about one quarter of the world's population killing roughly two million individuals per a year. Despite how ancient the disease is, the pathogen that causes Tuberculosis.
Now, research performed by scientists at the University of Rockefeller which is directed by Seth Darst and Elizabeth Campbell, a researcher in the Darst's laboratory, may challenge the evolutionary traits of M. tuberculosis offering a strong and potent treatment against the disease. The particular research has focused on an antibiotic that eradicates M. tuberculosis in a laboratory environment which is not suitable for clinical use. The researcher's work has aimed to explain how this new treatment operates which can encourage other investigators to develop new antibiotics to effectively treat tuberculosis patients.
Fidaxomicin works to inhibit an enzyme called RNA polymerase (RNAP), which helps transcribe DNA into RNA, a fundamental process of life. The enzyme, RNA polymerase, was seen to include hinged pincer that works to close down for secure DNA transcription. Therefore, investigators believe that fidaxomicin can interfere with the hinged pincer of the RNA polymerase, they just not yet understand how the interference occurs and if fidaxomicin holds inhibiting properties such knowledge may pride more versions of fidaxomicin for maximum efficacy against tuberculosis.
Furthermore, the research team took it a step furthers to work with a non-pathogenic cousin of M. tuberculosis; which is M. smegmatis. In particular, they used a mutant form of the bacterium that have a portion of the RbpA that is necessary for interaction with fidaxomicin. If the normal Mycobacteria was exposed to fidaxomicin, then the bacterium will not grow. On the other hand, the mutant forms were successful in dividing and thriving despite the presence of an antibiotic. This concluded that RbpA is essential in part of the mechanism which allows these un-mutated forms of Mycobacteria to be vulnerable to fidaxomicin.