ArticleProtein science : a publication of the Protein Society2021
A useful epitope tag derived from maltose binding protein.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 13 citations in OpenAlex.
- Molecular recognition and induced dimerization of hnRNP A2/B1 truncations by G-quadruplex single strand DNA.Scientific reports · 2026Article
- Precise mapping of two conserved minimal epitopes on the nucleocapsid protein of porcine epidemic diarrhea virus.Frontiers in microbiology · 2026Article
- The Achilles Heel of Protein Biochemistry: Insolubility of Recombinant Proteins-A Case Study About Producing a Rice Enzyme.International journal of molecular sciences · 2025Article
- Production of recombinant HPV11/16 E6/E7-MBP-HisVirology journal · 2024Article
- Tagging Recombinant Proteins to Enhance Solubility and Aid Purification.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Cloning and Expression of Heparinase Gene from a Novel Strain Raoultella NX-TZ-3-15.Applied biochemistry and biotechnology · 2022Article
- A useful epitope tag derived from maltose binding protein.Protein science : a publication of the Protein Society · 2021Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Maltose binding protein (MBP) is used in recombinant protein expression as an affinity and solubility tag. The monoclonal antibody B48 binds MBP tightly and has no cross-reactivity to other proteins in an Escherichia coli lysate. This high level of specificity suggested that MBP contains an epitope that could prove useful as a purification and visualization tag for proteins expressed in E. coli. To discover the MBP epitope, a co-crystal structure was determined for MBP bound to its antibody and four amino acids of MBP were identified as critical for the binding interaction. Fusions of various fragments of MBP to the glutathione S-transferase protein were engineered in order to identify the smallest fragment still recognized by the α-MBP antibody. Stabilization of the epitope via mutational engineering resulted in a minimized 14 amino-acid tag.
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