ArticleJournal of biological engineering2026
Natural diversity-guided catalytic-core chimerism engineers a rapid and inhibitor-tolerant reverse transcriptase.
Article in Journal of biological engineering, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundReverse transcriptases (RTs) are essential components of RNA-based molecular technologies, yet their practical performance is often constrained by trade-offs between catalytic speed, thermal stability, and tolerance to inhibitory substances. Conventional optimization via mutagenesis or directed evolution often improves individual traits but struggles to integrate multiple traits within a single enzyme. Here, we applied catalytic-core recombination, guided by natural sequence diversity and diagnostic performance criteria, to recover reverse transcriptase phenotypes that would be difficult to obtain by single-trait optimization alone.
resultsStarting from 1,028 sequences, 24 representative RT variants were used to generate a library of chimeras by swapping a critical 405-residue polymerase domain into a validated M-MuLV scaffold. We identified chRT V18 as the lead candidate, demonstrating consistent activity across a broad temperature range (40-70 °C). In addition, chRT V18 enabled efficient and linear cDNA synthesis in as little as 1 min at elevated temperatures, while maintaining strong resistance to clinically relevant inhibitors. Beyond RT-qPCR, chRT V18 supported high-temperature RT-LAMP at 69 °C, a regime typically incompatible with conventional RTs, enabling improved specificity and rapid amplification. When formulated into one-step RT-qPCR master mixes, chRT V18 achieved low limits of detection and full concordance with IVD-approved assays, while reducing reverse transcription time by 90%, enabling shorter time-to-result.
conclusionsNatural diversity-guided catalytic-core chimerism enabled the development of a rapid, inhibitor-tolerant reverse transcriptase with an unusual combination of broad temperature compatibility, minute-scale reverse transcription, and resilience to clinically relevant inhibitors. Beyond the properties of chRT V18 itself, the results support modular recombination of evolutionarily optimized domains as a practical engineering strategy for integrating multiple performance traits in complex enzymes.
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