ArticleNature communications2023
Mechanism of glycoform specificity and in vivo protection by an anti-afucosylated IgG nanobody.
Article in Nature communications, 2023. 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
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
12 citing papers in PubMed.
- Functional antibody responses and protection against symptomatic dengue.Communications medicine · 2026Review
- LeGenD: High-throughput N-glycan profiling using explainable AI and lectin profiling.The Journal of biological chemistry · 2026Article
- Glycoproteomic and genetic analysis of N-glycosylation of complement component C3 reveals immune pathway regulation.Genome biology · 2026Article
- Review
- Mechanisms of antibody-dependent enhancement of infectious disease.Nature reviews. Immunology · 2025Review
- COVID-19 vaccination induces cross-reactive dengue virus antibodies with altered isotype profiles andFrontiers in immunology · 2025Article
- Review
- Linking Effector Function to Antitumor Monoclonal Antibody Efficacy.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- LeGenD: determining N-glycoprofiles using an explainable AI-leveraged model with lectin profiling.bioRxiv : the preprint server for biology · 2024Article
- Current Insights Into K-associated Fetal Anemia and Potential Treatment Strategies for Sensitized Pregnancies.Transfusion medicine reviews · 2024Review
- Splenic macrophages escalate dengue disease.Nature microbiology · 2023Article
- Understanding antibody-dependent enhancement in dengue: Are afucosylated IgG1s a concern?PLoS pathogens · 2023Article
Corrections and comments
- Update of
Authors and funding
9 authors.
Funding
Abstract
Immunoglobulin G (IgG) antibodies contain a complex N-glycan embedded in the hydrophobic pocket between its heavy chain protomers. This glycan contributes to the structural organization of the Fc domain and determines its specificity for Fcγ receptors, thereby dictating distinct cellular responses. The variable construction of this glycan structure leads to highly-related, but non-equivalent glycoproteins known as glycoforms. We previously reported synthetic nanobodies that distinguish IgG glycoforms. Here, we present the structure of one such nanobody, X0, in complex with the Fc fragment of afucosylated IgG1. Upon binding, the elongated CDR3 loop of X0 undergoes a conformational shift to access the buried N-glycan and acts as a 'glycan sensor', forming hydrogen bonds with the afucosylated IgG N-glycan that would otherwise be sterically hindered by the presence of a core fucose residue. Based on this structure, we designed X0 fusion constructs that disrupt pathogenic afucosylated IgG1-FcγRIIIa interactions and rescue mice in a model of dengue virus infection.
Indexed as
Identifiers
What OpenQuestion holds
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.