Purification and characterization of anti-tubercular and anticancer protein from Staphylococcus hominis strain MANF2: In silico structural and functional insight of peptide

The present context was investigated to purify and characterize anti-tubercular as well as anticancer protein from fermented food associated Staphylococcus hominis strain MANF2. Initially, the anti-tubercular potency of strain MANF2 was assessed against Mycobacterium tuberculosis H37Rv using luciferase reporter phase assay which revealed pronounced relative light unit (RLU) reduction of 92.5 +/- 1.2%. The anticancer property of strain MANF2 was demonstrated against lung cancer (A549) and colon cancer (HT-29) cell lines using MIT assay which showed reduced viabilities. Anti-tubercular activities of the purified protein were observed to be increased significantly (P < 0.05) ranging from 34.6 +/- 0.3 to 71.4 +/- 0.4% of RLU reduction. Likewise, the purified protein showed significantly (P < 0.05) reduced viabilities of A549 and HT-29 cancer cells with IC50 values of 46.6 and 48.9 tig/mL, respectively. The nominal mass of the purified protein was found to be 7712.3 Da as obtained from MALDI-TOF MS/MS spectrum. The protein showed the sequence homology with 1-336 amino acids of Glyceraldehyde-3-phosphate dehydrogenase from Staphylococcus sp., thus, categorizing as a new class of Glyceraldehyde-3-phosphate dehydrogenase-like protein. The amino acid sequence of the most abundant peptide (m/z = 1922.12) in the purified protein was obtained as 'KAIGLVIPEIDGKLDGGAQRV' and it was identified as peptide NMANF2. In silico tools predicted significant stereo-chemical, physiochemical, and functional characteristics of peptide NMANF2. In a nutshell, protein purified from strain MANF2 can certainly be used as an ideal therapeutic agent against tuberculosis and cancer (lung and colon). (C) 2020 The Author(s). Published by Elsevier B.V. on behalf of King Saud University.