ArticleInfection and immunity1993
Mechanism of interaction of the 85B secreted protein of Mycobacterium bovis with fibronectin.
Article in Infection and immunity, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 59 citations in OpenAlex.
- Fusion Protein Vaccine Based on Ag85B and STEAP1 Induces a Protective Immune Response against Prostate Cancer.Vaccines · 2021Article
- Review
- Evaluation of a temperature-restricted, mucosal tuberculosis vaccine in guinea pigs.Tuberculosis (Edinburgh, Scotland) · 2018Article
- Surface proteome of "Mycobacterium avium subsp. hominissuis" during the early stages of macrophage infection.Infection and immunity · 2012Article
- Novel mycobacteria antigen 85 complex binding motif on fibronectin.The Journal of biological chemistry · 2012Article
- Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease.Infection and immunity · 2011Review
- Article
- Study on enhancement of fibronectin-mediated bacillus Calmette-Guérin attachment to urinary bladder wall in rabbits.World journal of urology · 2007Article
- FbpA-Dependent biosynthesis of trehalose dimycolate is required for the intrinsic multidrug resistance, cell wall structure, and colonial morphology of Mycobacterium smegmatis.Journal of bacteriology · 2005Article
- Secreted intestinal surfactant-like particles interact with cell membranes and extracellular matrix proteins in rats.The Journal of physiology · 2002Article
- Fibronectin facilitates Mycobacterium tuberculosis attachment to murine alveolar macrophages.Infection and immunity · 2002Article
- Fibronectin attachment protein homologue mediates fibronectin binding by Mycobacterium avium subsp. paratuberculosis.Infection and immunity · 2001Article
- Epitope focus, clonal composition and Th1 phenotype of the human CD4 response to the secretory mycobacterial antigen Ag85.Clinical and experimental immunology · 2001Article
- The domains of human fibronectin mediating the binding of alpha antigen, the most immunopotent antigen of mycobacteria that induces protective immunity against mycobacterial infection.The Biochemical journal · 2000Article
- Induction of monocyte expression of tumor necrosis factor alpha by the 30-kD alpha antigen of Mycobacterium tuberculosis and synergism with fibronectin.The Journal of clinical investigation · 1996Article
- T-cell determinants and antibody binding sites on the major mycobacterial secretory protein MPB59 of Mycobacterium bovis.Infection and immunity · 1994Article
- Gene for an extracellular matrix receptor protein from Pneumocystis carinii.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 85B protein of Mycobacterium bovis is a member of the secreted antigen 85 complex, which has been identified in a number of pathogenic mycobacteria. The 85 complex contains three components with molecular masses of 30 to 32 kDa which share the property of binding to fibronectin, a large glycoprotein present in plasma. To investigate this activity we have expressed the M. bovis 85B antigen as a recombinant protein and studied its interaction with human fibronectin. Fibronectin bound to the immobilized 85B protein in a solid-phase enzyme-linked immunosorbent assay (ELISA) and in the fluid phase in a radioimmunoassay using 125I-labelled 85B protein. In addition, fibronectin reacted with immobilized 85B in immunoblots and vice versa. Fibronectin also bound to three fragments of a cyanogen bromide digest of 85B which were subsequently identified by N-terminal sequencing. These fragments contained fibronectin-reactive peptides identified in ELISAs utilizing a set of 28 overlapping 20-mer peptides encompassing the 85B sequence. Further studies showed that the 85B protein reacted with a 32-kDa polypeptide from a limited tryptic digest of fibronectin which was identified as the collagen-binding domain. This region was confirmed as the 85B binding site by the fact that gelatin but not heparin inhibited the binding of fibronectin to 85B. These data indicate that the 85B-fibronectin interaction involves the binding of multiple regions of the 85B protein to the collagen-binding domain of fibronectin.
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