ArticleTuberculosis (Edinburgh, Scotland)2008
Identification of outer membrane proteins of Mycobacterium tuberculosis.
Article in Tuberculosis (Edinburgh, Scotland), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.
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Who cites it
89 citing papers in PubMed, 169 citations in OpenAlex.
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- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
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- Monoclonal Antibodies Targeting Bacillus Calmette-Guérin (BCG) Outer Membrane Proteins Confer Protection Against Tuberculosis.Transboundary and emerging diseases · 2026Article
- Contribution of Proteins to Membrane and Cell Wall Structures in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Mycobacterium tuberculosis TtfA is a Highly Stable Membrane-Anchored DNA-Binding Protein.The Journal of membrane biology · 2025Article
- Isolation and characterization of a protective monoclonal antibody targeting outer membrane protein (OmpA) against tuberculosis.Microbiology spectrum · 2025Article
- Different antibody isotypes against tuberculosis: what we know and what we need to know.Frontiers in immunology · 2025Review
- Comparative Proteomic Analysis of Cell Wall Proteins of Aminoglycosides Resistant and SensitiveCurrent protein & peptide science · 2025Article
- Glycan-mediated adhesion mechanisms in antibiotic-resistant bacteria.BBA advances · 2025Article
- Protease shaving ofbioRxiv : the preprint server for biology · 2024Article
- Whole Genome Sequencing Highlights the Pathogenic Profile in Nocardia Keratitis.Investigative ophthalmology & visual science · 2024Article
- Immunochemical characterisation of styrene maleic acid lipid particles prepared from Mycobacterium tuberculosis plasma membrane.PloS one · 2023Article
- FtsEX-independent control of RipA-mediated cell separation inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- In silico and in vitro study of Mycobacterium tuberculosis H37Rv uncharacterized protein (RipD): an insight on tuberculosis therapeutics.Journal of molecular modeling · 2022Article
- Chemical Reporters for Bacterial Glycans: Development and Applications.Chemical reviews · 2022Review
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- WNT6/ACC2-induced storage of triacylglycerols in macrophages is exploited by Mycobacterium tuberculosis.The Journal of clinical investigation · 2021Article
- Transporters Involved in the Biogenesis and Functionalization of the Mycobacterial Cell Envelope.Chemical reviews · 2021Review
29 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The cell wall of mycobacteria includes an unusual outer membrane of extremely low permeability. While Escherichia coli uses more than 60 proteins to functionalize its outer membrane, only two mycobacterial outer membrane proteins (OMPs) are known. The porin MspA of Mycobacterium smegmatis provided the proof of principle that integral mycobacterial OMPs share the beta-barrel structure, the absence of hydrophobic alpha-helices and the presence of a signal peptide with OMPs of gram-negative bacteria. These properties were exploited in a multi-step bioinformatic approach to predict OMPs of M. tuberculosis. A secondary structure analysis was performed for 587 proteins of M. tuberculosis predicted to be exported. Scores were calculated for the beta-strand content and the amphiphilicity of the beta-strands. Reference OMPs of gram-negative bacteria defined threshold values for these parameters that were met by 144 proteins of unknown function of M. tuberculosis. Two of them were verified as OMPs by a novel two-step experimental approach. Rv1698 and Rv1973 were detected only in the total membrane fraction of M. bovis BCG in Western blot experiments, while proteinase K digestion of whole cells showed the surface accessibility of these proteins. These findings established that Rv1698 and Rv1973 are indeed localized in the outer membrane and tripled the number of known OMPs of M. tuberculosis. Significantly, these results provide evidence for the usefulness of the bioinformatic approach to predict mycobacterial OMPs and indicate that M. tuberculosis likely has many OMPs with beta-barrel structure. Our findings pave the way to identify the set of proteins which functionalize the outer membrane of M. tuberculosis.
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