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Insights from the analysis of predicted Rv0679c protein peptide from Mycobacterium tuberculosis with Toll like
Rupa Lavarti1, Jayasree Ganugapati1, Shirisa Ratcha1
1Department of Biotechnology, Sreenidhi Institute of Science & Technology, Ghatkesar, Hyderabad - 501301.
Abstract:
Peptides of Rv0679c a membrane protein of the cell envelope (16.6 KDa) of Mycobacterium tuberculosis (M. tb), inhibited entry of live bacilli into epithelial (A549) and macrophage (U937) cell lines in vitro, suggesting a possible role in invasion. Receptors associated with Rv0679c antigen entry into cell lines were not characterized. We are reporting that Rv0679c peptides could bind to Toll like receptors (TLRs), the principal class of pathogen recognition receptors on host cells (PRR) by docking studies. Peptide structures were predicted using PEP FOLD and docking of truncated peptides with TLR's was performed using Cluspro 2.0. Docked complexes were analyzed using Swiss-PDB Viewer. Nine peptides of Rv0679c protein assessed were able to bind to TLR2-1 and TLR 4-MD2; however the binding energy was better with TLR 4-MD2. Peptide 30985 (-866.4 kcal/mol) has better binding energy with TLR2-1, in contrast peptide 30982 showed a better binding energy to TLR 4-MD2 dimer with a score of -1291.7 kcal/mol. Interactive residue analysis revealed that GLU 173 and SER 454 of TLR 1; ARG 447 and ARG 486 of TLR2; ARG 264 of TLR 4 and SER 120, LYS 122 and GLU 92 of MD2 region are predominant residues interacting with peptides of Rv0679c protein. Our study suggests that predominant residues and receptors of TLR2 and TLR4 are important for Rv0679c protein binding, which could further lead to invasion of M. tb into the host cell.
Insights
Rv0679c protein peptides from Mycobacterium tuberculosis bind to Toll-like receptors (TLRs), suggesting a mechanism for bacterial invasion into host cells. This interaction with TLR2 and TLR4 may be crucial for M. tb pathogenesis.
Area of Science:
- Immunology
- Microbiology
- Structural Biology
Background:
- Rv0679c is a membrane protein of Mycobacterium tuberculosis (M. tb).
- Peptides derived from Rv0679c inhibit M. tb entry into host cells, hinting at a role in invasion.
- The host cell receptors for Rv0679c are currently uncharacterized.
Purpose of the Study:
- To investigate the potential binding of Rv0679c peptides to host cell receptors.
- To identify specific Toll-like receptors (TLRs) involved in Rv0679c peptide interaction.
- To elucidate the binding interactions and energy between Rv0679c peptides and TLRs.
Main Methods:
- Peptide structures were predicted using PEP FOLD.
- Truncated Rv0679c peptides were docked with Toll-like receptors (TLRs) using Cluspro 2.0.
- Complexes were analyzed using Swiss-PDB Viewer for binding energy and residue interactions.
Main Results:
- Nine Rv0679c peptides demonstrated binding to TLR2-1 and TLR4-MD2.
- Peptide 30982 exhibited stronger binding energy to TLR4-MD2 (-1291.7 kcal/mol) than peptide 30985 to TLR2-1 (-866.4 kcal/mol).
- Key residues in TLR2 and TLR4-MD2, including GLU 173, SER 454, ARG 447, ARG 486, ARG 264, SER 120, LYS 122, and GLU 92, were identified as crucial for peptide binding.
Conclusions:
- Rv0679c peptides bind to TLR2 and TLR4 receptors.
- Specific residues on TLR2 and TLR4-MD2 are critical for this interaction.
- This binding interaction may facilitate M. tb invasion into host cells, highlighting a potential therapeutic target.
