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Monoclonal Antibodies Against UDP-N-Acetylglucosamine Enolpyruvyl Transferase From Mycobacterium Tuberculosis

Authors
Jin, Bong-Suk; Lee, Won-Kyu; Kim, Youngsun; Kim, Hongju; Kim, Hyejin; Ryoo, Sungweon; Hwang, Sung Chul
Department
Department of Pulmonary & Critical Care Medicine
Abstract
UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) catalyzes the biosynthesis of peptidoglycan, an essential ingredient of the bacterial cell wall. MurA from Mycobacterium tuberculosis shows the absence of homology with proteins in mammals. Therefore, it would potentially make an ideal target for anti-tuberculosis chemotherapy. We overexpressed M. tuberculosis MurA in Escherichia coli as the form of inclusion body, and it was denatured in a high concentration of urea. M. tuberculosis MurA with the high purity was prepared by the stepwise removal of urea and Ni-affinity chromatography. Ten monoclonal antibodies to M. tuberculosis MurA were prepared by the immunization to rabbit. Some of purified monoclonal antibodies activated or inhibited the M. tuberculosis MurA activity. Monoclonal antibodies against M. tuberculosis MurA will give a crucial key for its functional studies and rational design for inhibitor development.
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