ArticlePloS one2014
New tags for recombinant protein detection and O-glycosylation reporters.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
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- CRISPR-Csy4-Mediated Editing of Rotavirus Double-Stranded RNA Genome.Cell reports · 2020Article
- Conserved Rotavirus NSP5 and VP2 Domains Interact and Affect Viroplasm.Journal of virology · 2020Article
- DENV2 Pseudoviral Particles with Unprocessed Capsid Protein Are Assembled and Infectious.Viruses · 2019Article
- BiP/GRP78 Mediates ERAD Targeting of Proteins Produced by Membrane-Bound Ribosomes Stalled at the STOP-Codon.Journal of molecular biology · 2019Article
- Hit and go CAS9 delivered through a lentiviral based self-limiting circuit.Nature communications · 2017Article
- Rotavirus replication is correlated with S/G2 interphase arrest of the host cell cycle.PloS one · 2017Article
- Reduction of HIV-1 infectivity through endoplasmic reticulum-associated degradation-mediated Env depletion.Journal of virology · 2015Article
- Dengue E Protein Domain III-Based DNA Immunisation Induces Strong Antibody Responses to All Four Viral Serotypes.PLoS neglected tropical diseases · 2015Article
- An efficient system for bioconjugation based on a widely applicable engineered O-glycosylation tag.mAbsArticle
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monoclonal antibodies (mAbs), because of their unique specificity, are irreplaceable tools for scientific research. Precise mapping of the antigenic determinants allows the development of epitope tagging approaches to be used with recombinant proteins for several purposes. Here we describe a new family of tags derived from the epitope recognized by a single highly specific mAb (anti-roTag mAb), which was obtained from a pool of mAbs reacting with the rotavirus nonstructural protein 5 (NSP5). The variable regions of the anti-roTag mAb were identified and their binding capacity verified upon expression as a single-chain/miniAb. The minimal epitope, termed roTag, was identified as a 10 amino acid sequence (SISSSIFKNE). The affinity of the anti-roTag/roTag interaction was found to be comparable to that of the anti-SV5/SV5 tag interaction. roTag was successfully used for detection of several recombinant cytosolic, secretory and membrane proteins. Two additional variants of roTag of 10 and 13 amino acids containing O-glycosylation susceptible sites (termed OG-tag and roTagO) were constructed and characterised. These tags were useful to detect proteins passing through the Golgi apparatus, the site of O-glycosylation.
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