ArticleProceedings of the National Academy of Sciences of the United States of America2002
Mycobacterial heparin-binding hemagglutinin and laminin-binding protein share antigenic methyllysines that confer resistance to proteolysis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 121 citations in OpenAlex.
- Monoclonal Antibodies Targeting Bacterial Infections: A Broad Review of the Field.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- Nucleoid-associated protein HU constrains transcription elongation to influence cellular functions, virulence, and drug tolerance in Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- HBHA-ECSIT interaction disrupts macrophage autophagy to promote Mycobacterium tuberculosis persistence.Frontiers in immunology · 2025Article
- Recombinant mycobacterial DNA-binding protein 1 with post-translational modifications boosts IFN-gamma production from BCG-vaccinated individuals' blood cells in combination with CpG-DNA.Scientific reports · 2024Article
- Evaluation of cytokine profiles related toFrontiers in immunology · 2024Article
- Serological analysis reveals differential antibody responses between TB patients and latently infected individuals from the TB endemic country of Mozambique.Frontiers in medicine · 2023Article
- New Insights into the Methylation ofPathogens (Basel, Switzerland) · 2021Article
- TB or not to be: what specificities and impact do antibodies have during tuberculosis?Oxford open immunology · 2021Review
- Methylation of two-component response regulator MtrA in mycobacteria negatively modulates its DNA binding and transcriptional activation.The Biochemical journal · 2020Article
- Feature of Adhesins Produced by Human Clinical Isolates ofMicroorganisms · 2020Article
- G-Quadruplex-Forming DNA Aptamers Inhibit the DNA-Binding Function of HupB and Mycobacterium tuberculosis Entry into Host Cells.Molecular therapy. Nucleic acids · 2018Article
- Rv0613c/MSMEG_1285 Interacts with HBHA and Mediates Its Proper Cell-Surface Exposure in Mycobacteria.International journal of molecular sciences · 2018Article
- Posttranslational modification of a histone-like protein regulates phenotypic resistance to isoniazid in mycobacteria.Science advances · 2018Article
- A structural overview of mycobacterial adhesins: Key biomarkers for diagnostics and therapeutics.Protein science : a publication of the Protein Society · 2018Review
- Heparin-Binding Hemagglutinin Adhesin (HBHA) Is Involved in Intracytosolic Lipid Inclusions Formation in Mycobacteria.Frontiers in microbiology · 2018Article
- Article
- Involvement of methylated HBHA expressed from Mycobacterium smegmatis in an IFN-γ release assay to aid discrimination between latent infection and active tuberculosis in BCG-vaccinated populations.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2017Article
- Iron Homeostasis in Mycobacterium tuberculosis: Mechanistic Insights into Siderophore-Mediated Iron Uptake.Journal of bacteriology · 2016Review
- Multiple Posttranslational Modifications of Leptospira biflexa Proteins as Revealed by Proteomic Analysis.Applied and environmental microbiology · 2016Article
- Highly immunoreactive antibodies against the rHup-F2 fragment (aa 63-161) of the iron-regulated HupB protein of Mycobacterium tuberculosis and its potential for the serodiagnosis of extrapulmonary and recurrent tuberculosis.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2015Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacterium tuberculosis and Mycobacterium bovis bacillus Calmette-Guérin produce a heparin-binding hemagglutinin adhesin (HBHA) required for extrapulmonary dissemination and a laminin-binding protein (LBP) involved in cytoadherence through laminin recognition. These adhesins bear posttranslational modifications that are not present when the proteins are produced in a recombinant (r) form in Escherichia coli. Mass spectrometry analysis of HBHA revealed that the posttranslational modifications are borne by the C-terminal moiety, which comprises the heparin-binding domain made of repeated lysine-rich motifs. Amino acid sequencing showed that these modifications consist of mono- and dimethyllysines within these motifs. The methyllysine-containing repeats were recognized by mAb 4057D2 and were also detected in LBP, which is equally recognized by mAb 4057D2. This Ab does not recognize the recombinant forms of these proteins. However, when rHBHA and rLBP were subjected to NaBH(4) and formalin treatment to induce lysine methylation, reactivity with mAb 4057D2 was recovered. Methylated rHBHA displayed enhanced resistance to proteolysis compared with rHBHA, as previously observed for native HBHA. S-adenosylmethionine-dependent HBHA methyltransferase activity was detected in the cell-wall fractions of M. bovis bacillus Calmette-Guérin and of Mycobacterium smegmatis, a species that produces LBP but naturally lacks hbhA, suggesting that the same enzyme(s) methylate(s) both LBP and HBHA. This hypothesis was confirmed by the fact that HBHA produced by recombinant M. smegmatis was also methylated. These results show that mycobacteria use enzymatic methylation of lysines to ensure greater stability of their adhesins.
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