ArticleJournal of biochemistry2020
Site-specific epitope insertion into recombinant proteins using the MAP tag system.
Article in Journal of biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis.Nature cell biology · 2026Article
- SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis.bioRxiv : the preprint server for biology · 2026Article
- EMab-300 Detects Mouse Epidermal Growth Factor Receptor-Expressing Cancer Cell Lines in Flow Cytometry.Antibodies (Basel, Switzerland) · 2023Article
- Development of a Novel Anti-CD44 Variant 7/8 Monoclonal Antibody, CBiomedicines · 2023Article
- Epitope Mapping of Anti-Mouse CCR3 Monoclonal Antibodies Using Flow Cytometry.Antibodies (Basel, Switzerland) · 2022Article
- Development of a Novel Anti-CD44 Monoclonal Antibody for Multiple Applications against Esophageal Squamous Cell Carcinomas.International journal of molecular sciences · 2022Article
- DogCatcher allows loop-friendly protein-protein ligation.Cell chemical biology · 2022Article
- A hemolysin secretion pathway-based novel secretory expression platform for efficient manufacturing of tag peptides and anti-microbial peptides in Escherichia coli.Bioresources and bioprocessing · 2021Article
- Lasso-grafting of macrocyclic peptide pharmacophores yields multi-functional proteins.Nature communications · 2021Article
- RIEDL tag: A novel pentapeptide tagging system for transmembrane protein purification.Biochemistry and biophysics reports · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The MAP tag system comprises a 14-residue peptide derived from mouse podoplanin and its high-affinity monoclonal antibody PMab-1. We determined the crystal structure of PMab-1 complexed with the MAP tag peptide and found that the recognition required only the N-terminal 8 residues of MAP tag sequence, enabling the shortening of the tag length without losing the affinity for PMab-1. Furthermore, the structure illustrated that the MAP tag adopts a U-shaped conformation when bound by PMab-1, suggesting that loop-inserted MAP tag would assume conformation compatible with the PMab-1 binding. We inserted the 8-residue MAP tag into multiple loop regions in various proteins including fibronectin type III domain and G-protein-coupled receptors and tested if they maintain PMab-1 reactivity. Despite the conformational restraints forced by the insertion position, all MAP-inserted mutants were expressed well in mammalian cells at levels comparable to the non-tagged proteins. Furthermore, the binding by PMab-1 was fully maintained even for the mutant where MAP tag was inserted at a structurally restricted β-hairpin, indicating that the MAP tag system has unique feature that allows placement in the middle of protein domain at desired locations. Our results indicate the versatile utility of the MAP tag system in 'site-specific epitope insertion' application.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.