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Enrichment of Native and Recombinant Extracellular Vesicles of Mycobacteria
Published on: December 8, 2023
Mycobacterium tuberculosis Rv0679c protein sequences involved in host-cell infection: potential TB vaccine candidate
Diana P Cifuentes1, Marisol Ocampo, Hernando Curtidor
1Fundación Instituto de Inmunología de Colombia, Carrera 50 No, 26-20, Bogotá, Colombia.
Background:
To date, the function of many hypothetical membrane proteins of Mycobacterium tuberculosis is still unknown and their involvement in pathogen-host interactions has not been yet clearly defined. In this study, the biological activity of peptides derived from the hypothetical membrane protein Rv0679c of M. tuberculosis and their involvement in pathogen-host interactions was assessed. Transcription of the Rv0679c gene was studied in 26 Mycobacterium spp. Strains. Antibodies raised against putative B-cell epitopes of Rv0679c were used in Western blot and immunoelectron microscopy assays. Synthetic peptides spanning the entire length of the protein were tested for their ability to bind to A549 and U937 cells. High-activity binding peptides (HABPs) identified in Rv0679c were tested for their ability to inhibit mycobacterial invasion into cells.
Results:
The gene encoding Rv0679c was detected in all strains of the M. tuberculosis complex (MTC), but was only transcribed in M. tuberculosis H37Rv, M. tuberculosis H37Ra and M. africanum. Anti-Rv0679c antibodies specifically recognized the protein in M. tuberculosis H37Rv sonicate and showed its localization on mycobacterial surface. Four HABPs inhibited invasion of M. tuberculosis to target cells by up to 75%.
Conclusions:
The results indicate that Rv0679c HABPs and in particular HABP 30979 could be playing an important role during M. tuberculosis invasion of host cells, and therefore could be interesting research targets for studies aimed at developing strategies to control tuberculosis.
Insights
Researchers explored peptides from Mycobacterium tuberculosis Rv0679c protein to understand their role in host cell invasion. Specific peptides effectively inhibited bacterial entry, suggesting potential therapeutic targets for tuberculosis control.
Area of Science:
- Microbiology
- Immunology
- Protein Science
Background:
- Many Mycobacterium tuberculosis membrane proteins, including Rv0679c, have unknown functions and roles in host interactions.
- Understanding these proteins is crucial for developing new tuberculosis control strategies.
Purpose of the Study:
- To investigate the biological activity of peptides derived from the hypothetical membrane protein Rv0679c.
- To assess the involvement of Rv0679c in pathogen-host interactions and mycobacterial invasion.
Main Methods:
- Studied Rv0679c gene transcription across 26 Mycobacterium spp. strains.
- Utilized Western blot and immunoelectron microscopy with anti-Rv0679c antibodies.
- Tested synthetic peptides for cell binding and inhibition of M. tuberculosis invasion.
Main Results:
- Rv0679c gene was detected in all M. tuberculosis complex strains, with transcription observed in specific strains (M. tuberculosis H37Rv, H37Ra, M. africanum).
- Anti-Rv0679c antibodies confirmed protein localization on the mycobacterial surface.
- Four high-activity binding peptides (HABPs) inhibited M. tuberculosis invasion into host cells by up to 75%.
Conclusions:
- Rv0679c HABPs, particularly HABP 30979, play a significant role in M. tuberculosis host cell invasion.
- These HABPs represent promising research targets for developing novel tuberculosis control strategies.
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