ArticleScientific reports2017
Protection of Human Colon Cells from Shiga Toxin by Plant-based Recombinant Secretory IgA.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Effects of various disaccharide adaptations on recombinant IgA1 production in CHO-K1 suspension cells.Cytotechnology · 2023Article
- Prevention of Shiga toxin 1-caused colon injury by plant-derived recombinant IgA.Scientific reports · 2022Article
- Plant-derived secretory component gives protease-resistance to Shiga toxin 1-specific dimeric IgA.Plant molecular biology · 2021Article
- IgA as a potential candidate for enteric monoclonal antibody therapeutics with improved gastrointestinal stability.Vaccine · 2020Article
- Review
- Article
- Treatment Strategies for Infections With Shiga Toxin-ProducingFrontiers in cellular and infection microbiology · 2020Review
- Article
- Transformation strategies for stable expression of complex hetero-multimeric proteins like secretory immunoglobulin A in plants.Plant biotechnology journal · 2019Article
- Plant-derived secretory component forms secretory IgA with shiga toxin 1-specific dimeric IgA produced by mouse cells and whole plants.Plant cell reports · 2019Article
- Plant-Produced Chimeric VFrontiers in plant science · 2019Article
- Shiga Toxin Glycosphingolipid Receptors in Human Caco-2 and HCT-8 Colon Epithelial Cell Lines.Toxins · 2017Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Shiga toxin is a major virulence factor of food-poisoning caused by Escherichia coli such as O157:H7. Secretory immunoglobulin (Ig) A (SIgA) is supposed to prevent infection of the mucosal surface and is a candidate agent for oral immunotherapy. We previously established a recombinant monoclonal antibody (mAb) consisting of variable regions from a mouse IgG mAb specific for the binding subunit of Shiga toxin 1 (Stx1) and the Fc region of mouse IgA. Here we produced a secretory form of the recombinant IgA (S-hyIgA) with transgenic Arabidopsis thaliana plant. All the S-hyIgA cDNAs (heavy, light, J chain and secretory component) were expressed under the control of a bidirectional promoter of a chlorophyll a/b-binding protein of A. thaliana without using a viral promoter. The plant-based S-hyIgA exhibited antigen binding, and was modified with plant-specific N-linked sugar chains. The Ig heavy chain and secretory components were observed in an intracellular protein body-like structure of the transgenic leaves on immuno-electron microscopy. An extract of the transgenic leaves neutralized the cytotoxicity of Stx1 toward butyrate-treated Caco-2 cells, a human colon carcinoma cell line. These results will contribute to the development of edible therapeutic antibodies such as those for the treatment of mucosal infection.
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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.