ArticleMicrobial biotechnology2026
Deep Learning-Enabled Engineering of a Hyper-Stable and Soluble MPB70-83 Antigen for Sensitive Bovine Tuberculosis Surveillance.
Article in Microbial biotechnology, 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
16 authors.
Funding
Abstract
Bovine tuberculosis (bTB) diagnostics are frequently hindered by the structural instability and insolubility of recombinant multi-epitope proteins in prokaryotic expression systems. To address this, we developed an integrated strategy combining immunoinformatics with the ProteinMPNN deep learning framework. We constructed a fusion protein utilizing B-cell epitopes from MPB70 and MPB83, where ProteinMPNN was employed to redesign non-epitope scaffolds for optimized thermodynamic stability. The structural integrity was verified via 200-ns molecular dynamics (MD) simulations. MD analysis revealed the redesigned construct transitions into a rigid, compact native state with a stable hydrophobic core. Validating this in silico design, the optimized protein achieved high-yield soluble expression in Escherichia coli, eliminating inclusion body formation. The resulting indirect ELISA demonstrated 96.30% sensitivity and 98.61% specificity, showing excellent concordance (Cohen's κ > 0.9) with standard assays. This study demonstrates that deep learning-based sequence redesign effectively resolves solubility bottlenecks in antigen engineering, providing a robust, scalable tool for precision bTB surveillance.
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.