Neisseria gonorrhoeae is a pathogenic bacterium that causes the sexually transmitted disease gonorrhoea. Its ability to evade the immune system and causes recurrent infec-tions poses challenges in disease treatment. The current treatment with cephalosporins is becoming increasingly ineffective due to the emergence of resistant strains in Asia, Eu-rope, and North America, making the identification of new target proteins imperative. The Obg protein is an evolutionarily conserved GTPase responsible for the bacterial re-sponse to stress, chromosome separation, and ribosome maturation. It binds to the ribo-somal 50S subunit and, upon GTP hydrolysis, induces proper folding of the subunit. When the obg gene is knocked out, bacterial survival drastically decreases. The gene sequence for obg was inserted into the pMSCG7 vector using IVA cloning. We then isolated the construct from E. coli DH5α cells and introduced it into the expression strain of E. coli BL21 [DE3] pLys-S. After determining the optimal expression tempera-ture at 37 °C, we expressed and isolated approximately 30 mg of protein. We attempted to crystallise a small quantity of the purified protein, and the results are still pending. In subsequent work, we will identify conditions for the growth of this protein's crystals and determine its structure.
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