ArticleBMC infectious diseases2014
A peptide fragment from the human COX3 protein disrupts association of Mycobacterium tuberculosis virulence proteins ESAT-6 and CFP10, inhibits mycobacterial growth and mounts protective immune response.
Article in BMC infectious diseases, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Antimicrobial peptides for tuberculosis in a post-antibiotic era: from in vitro promise to therapeutic potential.npj antimicrobials and resistance · 2026Review
- Secreted proteins ofFrontiers in tuberculosis · 2026Review
- Peptide-Based Strategies AgainstPharmaceuticals (Basel, Switzerland) · 2025Review
- TargetingiScience · 2024Article
- Review
- Antimicrobial peptides as drugs with double response againstFrontiers in microbiology · 2023Review
- EST12 regulates Myc expression and enhances anti-mycobacterial inflammatory responseFrontiers in immunology · 2022Article
- Antimicrobial Peptides as Potential Anti-Tubercular Leads: A Concise Review.Pharmaceuticals (Basel, Switzerland) · 2021Review
- A De novo Peptide from a High Throughput Peptide Library Blocks Myosin A -MTIP Complex Formation inInternational journal of molecular sciences · 2020Article
- Human Cyclophilin B forms part of a multi-protein complex during erythrocyte invasion by Plasmodium falciparum.Nature communications · 2017Article
- Vaccine research and development: tuberculosis as a global health threat.Central-European journal of immunology · 2017Review
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTuberculosis (TB) is one of the most prevalent infectious diseases affecting millions worldwide. The currently available anti-TB drugs and vaccines have proved insufficient to contain this scourge, necessitating an urgent need for identification of novel drug targets and therapeutic strategies. The disruption of crucial protein-protein interactions, especially those that are responsible for virulence in Mycobacterium tuberculosis - for example the ESAT-6:CFP10 complex - are a worthy pursuit in this direction.
methodsWe therefore sought to improvise a method to attenuate M. tuberculosis while retaining the latter's antigenic properties. We screened peptide libraries for potent ESAT-6 binders capable of dissociating CFP10 from ESAT-6. We assessed the disruption by a peptide named HCL2, of the ESAT-6:CFP10 complex and studied its effects on mycobacterial survival and virulence.
resultsWe found that HCL2, derived from the human cytochrome c oxidase subunit 3 (COX3) protein, disrupts ESAT-6:CFP10 complex, binds ESAT-6 potently, disintegrates bacterial cell wall and inhibits extracellular as well as intracellular mycobacterial growth. In addition, an HCL2 expressing M. tuberculosis strain induces both Th1 and Th17 host protective responses.
conclusionsDisruption of ESAT-6:CFP10 association could, therefore, be an alternate method for attenuating M. tuberculosis, and a possible route towards future vaccine generation.
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