ArticleInternational journal of molecular sciences2013
Functional expression of thyroid-stimulating hormone receptor on nano-sized bacterial magnetic particles in Magnetospirillum magneticum AMB-1.
Article in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- Nanoparticles in Thyroid Autoimmunity: Diagnostic and Therapeutic Applications.Journal of clinical medicine · 2026Review
- OrthogonalApplied and environmental microbiology · 2025Article
- Magnetizing Biotech-Advances in (In Vivo) Magnetic Enzyme Immobilization.Engineering in life sciences · 2025Review
- Improved methods for mass production of magnetosomes and applications: a review.Microbial cell factories · 2020Review
- Bioengineered Polyhydroxyalkanoates as Immobilized Enzyme Scaffolds for Industrial Applications.Frontiers in bioengineering and biotechnology · 2020Review
- Functional expression of full-length TrkA in the prokaryotic host Magnetospirillum magneticum AMB-1 by using a magnetosome display system.Applied and environmental microbiology · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The measurement of autoantibodies to thyroid-stimulating hormone receptor (TSHR) is important for the diagnosis of autoimmune thyroid disease such as Graves' disease (GD). Although TSHR from porcine thyroid membrane is commonly used for the measurement of TSHR autoantibodies (TRAb), recombinant human TSHR (hTSHR) remains ideal in terms of stable supply and species identity. Here we set out to express recombinant hTSHR on the lipid-bilayer surface of magnetic nanoparticles from a magnetotactic bacterium, Magnetospirillum magneticum AMB-1. Using a tetracycline-inducible expression system, we successfully overexpressed functional hTSHR on bacterial magnetic particles (BacMPs) in AMB-1 via an anchor protein specific for BacMPs. The overexpressed hTSHR was membrane integrated and possessed both ligand and autoantibody binding activity. Our data suggest that hTSHR-displayed BacMPs have potential as novel tools for ligand-receptor interaction analysis or for TRAb immunoassay in GD patients.
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Registered trials
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