ArticleBiotechnology letters2012
Novel system for in vivo biotinylation and its application to crab antimicrobial protein scygonadin.
Article in Biotechnology letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Article
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- Isolation and Characterization of Single-Domain Antibodies from Immune Phage Display Libraries.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Adenovirus Fibers as Ultra-Stable Vehicles for Intracellular Nanoparticle and Protein Delivery.Biomolecules · 2022Article
- Labeling Cell Surface Receptors with Ligand.BirA* Bispecifics.ACS pharmacology & translational science · 2022Article
- Efficient isolation of rare B cells using next-generation antigen barcoding.Frontiers in cellular and infection microbiology · 2022Article
- Interactions of ubiquitin and CHMP5 with the V domain of HD-PTP reveals role for regulation of Vps4 ATPase.Molecular biology of the cell · 2021Article
- Redox Protein OsaR (PA0056) RegulatesAntimicrobial agents and chemotherapy · 2021Article
- Expression of in vivo biotinylated recombinant antigens SAG1 and SAG2A from Toxoplasma gondii for improved seroepidemiological bead-based multiplex assays.BMC biotechnology · 2020Article
- The chaperone SmgGDS-607 has a dual role, both activating and inhibiting farnesylation of small GTPases.The Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
BirA is a biotin ligase from Escherichia coli that specifically biotinylates a lysine side-chain within a 15-amino acid acceptor peptide (also known as Avi-tag). We developed a protocol for producing recombinant BirA ligase in E. coli for in vitro biotinylation (Li and Sousa, Prot Expr Purif, 82:162-167, 2012) in which the target protein was expressed as both thioredoxin and MBP fusions, and was released by TEV protease-mediated cleavage. The liberated ligase and the fusion proteins were enzymatically active. Based on that observation, we have now developed a novel system for in vivo biotinylation by co-expressing the Avi-tagged target protein with the MBP-BirA fusion. The effectiveness of this system was demonstrated by the successful in vivo labeling of antimicrobial protein, scygonadin. This new system shows improved efficiency compared with pre-existing one and this is likely attributed to the high expression level and solubility of the co-expressed MBP-BirA.
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Registered trials
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