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The Mycobacterial antigen 85 complex consists of three secreted proteins (Ag85A, Ag85B, Ag85C) that are crucial for the synthesis and maintenance of the mycobacterial outer membrane, conferring both structural integrity and resistance to chemotherapeutic agents. These enzymes catalyze essential reactions transferring mycolic acids between trehalose monomycolate molecules, ultimately forming the key cell wall components of Mycobacterium tuberculosis. The Ag85 complex is accessible for drug targeting due to its extracellular localization, making it an attractive target for novel antitubercular drugs, which may inhibit its enzymatic activity to compromise cell wall synthesis and mycobacterial viability
Drugs such as ebselen inhibit Ag85 by covalently binding to active site cysteines, disrupting catalytic activity essential for cell wall synthesis, thereby killing or inhibiting mycobacteria
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