RT Journal Article SR Electronic T1 In Silico analysis of PE_PGRS20 (Rv1068c) protein in Mycobacterium tuberculosis H37Rv JF bioRxiv FD Cold Spring Harbor Laboratory SP 2021.08.31.458215 DO 10.1101/2021.08.31.458215 A1 Saleem Ahmad A1 AnupKumar Kesavan YR 2021 UL http://biorxiv.org/content/early/2021/09/01/2021.08.31.458215.abstract AB The genetic makeup of Mycobacterium tuberculosis reveals the presence of an unknown repeat sequence of PE_PGRS family proteins that are responsible for antigenic variations and many unknown functions that includes necrosis of macrophage and apoptosis. The structure and function of these glycine-rich proteins can be predictable by homology modeling, the Ab-initio method, or by using different tools of bioinformatics. In this study, we selected, PE_PGRS20 (Rv1068c) an unknown PE_PGRS protein. We suggest that the PE_PGRS20 gene is linked with the others genes of the espACD operon which are the virulence factors in the M. tuberculosis H37Rv strain. The genes associated with this protein secretion system can perform the synthesis of a special type of fatty acid known as phthioceroldimycocerates (PDIM).Docking with different anti TB drugs shows binding with PE_PGRS20 protein which suggests that the target protein may involve in the drug resistance.Competing Interest StatementThe authors have declared no competing interest.