STUDY OF THE INTERACTION OF COLD SHOCK PROTEINS FROM MYCOBACTERIUM TUBERCULOSIS WITH SRNAS

Tuberculosis is a common infection affecting both humans and animals. The disease is caused by various strains of Mycobacterium tuberculosis, which causes about two million deaths worldwide each year. Once infiltrated into the host, mycobacteria inhibit autophagy and intercellular signaling, they are also resistant to toxic substances, which ensures their survival within macrophages. M. tuberculosis exhibits a high degree of genetic diversity, which contributes to their resistance to drugs. The emergence of multidrug-resistant strains (MDRTB) is a serious public health problem, complicating the diagnosis and treatment of the disease. Drugs used to control TB often require a long therapeutic regimen, increasing the risk of side effects. Understanding the mechanisms by which mycobacteria evade the immune response opens new horizons for the development of vaccines and more effective therapeutic approaches. For example, one of the survival strategies of this pathogen is the presence of multiple small regulatory RNAs (mRNAs) that form complex regulatory networks with mRNAs, helping the bacterium to rapidly and efficiently adapt its metabolism at different stages of infection. Normally, the process of translation regulation involving small regulatory RNAs is actively supported by RNA chaperones, proteins that promote the unraveling of the RNA secondary structure and the interaction of different RNA molecules such as mRNA and mRNA. Since the known and most studied RNA chaperones Hfq and ProQ were not found in mycobacteria, there is an assumption that this role may be performed by other RNA-binding proteins, such as members of the CspA/CspB protein family.