ArticleACS omega2026
Potent Cross-Serotype Dengue Neutralization with Low ADE by AG-Strand-Targeting Anti-EDIII Antibodies.
Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dengue virus (DENV) envelope protein domain III (EDIII) is a premier target for vaccine design because EDIII-specific antibodies can potently neutralize DENV with a low propensity for inducing antibody-dependent enhancement (ADE). We previously identified a cross-reactive antibody, R3N_2D3, which targets the EDIII AG-strand epitope and neutralizes all four DENV serotypes with low ADE, a desirable combination of activities among anti-DENV antibodies. In this study, we expanded this AG-strand-targeting antibody panel by identifying four additional anti-EDIII antibodies from our dengue-immune single-chain variable fragment (scFv)-phage libraries. Despite variations in their binding footprints, these new antibodies converged on key residues within the AG-strand epitope. When expressed as full IgG1, these candidates showed potent cross-neutralization with subnanomolar focus reduction neutralization titers (FRNT
Identifiers
What Socratic 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 Socratic graph.