ArticleScientific reports2026
AI-aided engineering and production optimization of chimeric hetero-viral capping enzymes for mRNA vaccines.
Article in Scientific reports, 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
5 authors.
Funding
Abstract
The 5’ cap structure exerts profound impacts on mRNA vaccine stability, translational efficiency, and evasion of innate immunity, encompassing key enzymatic components: triphosphatase (TPase), guanylyl transferase (GTase), and bifunctional methyltransfer-ases (N7G-MTase/2’-O-MTase). However, conventional multi-enzyme capping systems for mRNA vaccines are plagued by inherent inefficiencies. Herein, we report an AI-driven novel hetero-viral chimeric capping enzyme for mRNA vaccines, developed through bioinformatics mining of the DeepSeek and UniProt databases. This single-molecule biocatalyst integrates all capping functions by fusing a rabbit fibroma virus (RFV)-derived TPase/GTase domain with bifunctional methyltransferase domains from flavivirus (FV), respiratory syncytial virus (RSV), and rotavirus (RV). Following systematic tag-host optimization, a soluble and functional RFV-FV chimera was achieved via N-terminal maltose-binding protein (MBP) fusion in E. coli BL21(DE3) pLysS, whereas RFV-RSV and RFV-RV chimeras formed insoluble aggregates or were trapped in chaperone complexes. Complementary assays confirmed that the RFV-FV capping enzyme exhibited catalytic activities comparable to the commercial vaccinia virus-derived capping enzyme: TPase (96.76%±1.63%), GTase (100.69%±2.95%), and MTase (77.87%±3.85%). Our work presents a versatile cross-viral RFV-FV capping enzyme that enables large-scale prokaryotic production and ensures mRNA vaccine quality via its multifunctional catalytic activity, thereby streamlining mRNA vaccine manufacturing and establishing an AI-driven paradigm for designer enzyme engineering.
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.