ArticleFrontiers in immunology2025
Unlocking binding properties of single-domain antibodies targeting the polymeric immunoglobulin receptor to enhance mucosal enrichment of IgG against respiratory syncytial virus.
Article in Frontiers in immunology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers, 1 of them a synthesis that pooled it.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Associations Between Peripheral Blood Inflammatory and Immune Markers and Osteoporotic and Fragility Fractures: A Systematic Review and Meta-Analysis.Calcified tissue international · 2026Pooled it
- A review of bloodstream infections-pathogens, pathogenesis, diagnostic strategies, treatment methods-challenges and future aspects.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026Review
- Single-cell eQTL-based Mendelian randomization identifies immune cell subtype-specific regulators of epigenetic aging and prioritizes candidate therapeutic targets.Biogerontology · 2026Review
Corrections and comments
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Authors and funding
19 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A major driver of mucosal immunity is immunoglobulin A (IgA) that can translocate across mucosal epithelial barriers to protect against various pathogens in luminal spaces of the human body. The transcytosis of IgA is primarily mediated by the polymeric Ig receptor (pIgR), which is highly expressed in mucosal tissues and selectively transports polymeric IgA, but not IgG. IgG has been the preferred immunoglobulin isotype for therapeutic development because of its well-characterized biological functions and established manufacturing processes. Efficient transport of IgG across the epithelium into mucosal spaces is a highly desirable feature in the development of IgG-based neutralizing antibodies targeting respiratory infections. To address this challenge, we report discovery and characterization of anti-pIgR variable single-domain antibodies (V
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Registered trials
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.