Mycobacterium tuberculosis Rv0292 Protein Peptides Could be Included in a Synthetic Anti-tuberculosis Vaccine

Purpose This study was aimed at characterising Mycobacterium tuberculosis ( Mtb ) H37Rv Rv0292 protein peptides. As this protein forms a structural part of the cell wall and Mtb type VII secretion system, it is believed that Rv0292 has important functions regarding the disease’s pathogenesis and could represent a good candidate when designing a synthetic anti-tuberculosis vaccine. Methods Receptor-ligand binding assays were used for identifying peptides from the Rv0292 protein sequence having high specific binding activity (HABP) to infection target cells; some HABPs were able to inhibit Mtb H37Rv entry to such cell lines in in vitro assays. Fluorescent microsphere internalisation assays were carried out for corroborating such peptides’ role in mycobacterial entry. The protein’s predicted alfa helical structure was confirmed by circular dichroism of the peptides forming its sequence. Results It was found that peptide 31050 ( 101 LTLIARYLDRYGIRADTIRI 120 ) had high binding capacity for the cell lines used here and inhibited mycobacterial entry to such cell lines; it was also found that this peptide was not recognised by sera from individuals who had been in contact with the mycobacteria. Conclusions The aforementioned characteristics led to suggesting that peptide 31050 sequence plays an important role in Mtb H37Rv Rv0292 protein interaction with infection target cells and could be considered a candidate when designing a synthetic anti-tuberculosis vaccine.