ArticleBiophysical journal2025
Epitope mapping of diagnostic antibodies targeting SARS-CoV-2 nucleocapsid protein using hydrogen-deuterium exchange mass spectrometry.
Article in Biophysical journal, 2025. 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
9 authors.
Funding
Abstract
The SARS-CoV-2 nucleocapsid (N) protein is a primary target for diagnostic antibody-based detection of COVID-19. To enhance diagnostic accuracy and resilience against emerging variants, it is essential to map the binding sites of diagnostic antibodies. This study employs hydrogen-deuterium exchange mass spectrometry (HDX-MS) to identify the epitopes of diagnostic antibodies targeting the N protein. HDX-MS provides high-resolution insights into protein-antibody interactions by detecting changes in solvent accessibility and protein dynamics upon antibody binding. Our findings revealed distinct epitopes critical for antibody specificity and binding, highlighting conserved regions of the N protein that are crucial for diagnostic applications. This work demonstrates the value of HDX-MS in guiding the design of robust diagnostic tools, emphasizing its role in understanding antibody interactions and adapting diagnostics to future SARS-CoV-2 variants. These findings support the development of next-generation diagnostics with improved sensitivity, specificity, and durability.
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.