ArticleInfection and immunity1997
Murine antibody responses to the verotoxin 1 B subunit: demonstration of major histocompatibility complex dependence and an immunodominant epitope involving phenylalanine 30.
Article in Infection and immunity, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Shiga Toxin: Emerging Producer Strains, Prophylactic Approaches, and Application in Cancer Therapy.Journal of cancer prevention · 2024Review
- Shiga Toxins as Antitumor Tools.Toxins · 2021Review
- Review
- Protein toxins: intracellular trafficking for targeted therapy.Gene therapy · 2005Review
- Production of secretory immunoglobulin A against Shiga toxin-binding subunits in mice by mucosal immunization.Infection and immunity · 2004Article
- Mouse toxicity and cytokine release by verotoxin 1 B subunit mutants.Infection and immunity · 2001Article
- Antiviral activity of shiga toxin 1: suppression of bovine leukemia virus-related spontaneous lymphocyte proliferation.Infection and immunity · 2000Article
- Development of recombinant B subunit of Shiga-like toxin 1 as a probe to detect carbohydrate ligands in immunochemical and flowcytometric application.Glycoconjugate journal · 1999Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structurally conserved verotoxin 1 (VT1) mutant derivatives, showing reduced receptor binding and cytotoxicity, may serve as natural toxoids to protect against VT-mediated disease. In this study, the antibody responses to the wild-type VT1 B subunit, a B-subunit mutant (Phe30Ala B), and the corresponding holotoxin (Phe30Ala HT) were examined in three inbred mouse strains. BALB/c (H-2d) and CBA (H-2k) mice produced strong antibody responses to both wild-type and mutant B subunits. VT1 B-raised sera reacted more strongly with VT1 B than with Phe30Ala B in enzyme-linked immunosorbent assays, while Phe30Ala B-raised sera reacted equally with VT1 B and Phe30Ala B. C57BL/6 (H-2b) and congenic BALB/c (BALB x B [H-2b]) mice produced no detectable antibody response to either VT1 B or Phe30Ala B. However, an anti-VT1 B antibody response was detected in H-2b mice immunized with biologically active Phe30Ala HT. Based on these observations, we conclude that the VT1 B subunit possesses a B-cell immunodominant epitope formed partly by phenylalanine 30 and that the B-subunit antibody response is dependent on the H-2 haplotype of the mouse strain. Our results also support a potential role for the A subunit in providing the T-cell help necessary to overcome a deficient B-subunit antibody response in H-2b mice.
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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.