The study results are published in the Proceedings of the National Academy of Sciences (PNAS). Matthias Wilmanns, Head of EMBL Hamburg reveals the dangerousness and persistence of the bacteria M. tuberculosis. The functions of tuberculosis proteins and their atomic structures are investigated to develop inhibitors against the proteins. It was found that a protein, LipB is necessary as it activates cellular machines that drive the bacterium's metabolism. Stefan Kaufmann's department at the MPIIB has found that a 70 fold increase in LipB in patients infected by multidrug-resistant forms of M. tuberculosis.
Hence it plays a key role in the development of various new drug targets. A structural picture of the protein in the form of a technical diagram is being built which is of great importance. Qingjun Ma from Wilmann's group used high-energy synchrotron radiation beamlines and created an atom-by-atom map of the protein's structure. With the help of the high-resolution picture it was found how LipB attaches specific fatty acids onto other proteins. Wilmanns said that LipB is a very promising drug target as M. tuberculosis has no backup mechanism that could take over LipB's role. The scientists are now searching for drugs that inhibit the active site and prevent the bacterium ability to survive and replicate.