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| http://dx.doi.org/10.1038/nmeth.3588 | DOI Listing |
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Protein engineering enables Serratia marcescens nuclease A to hydrolyze nucleic acids under high-salt conditions.
Int J Biol Macromol
December 2024
Synthetic Biology Department, WuXi Biologics, 1951 Huifeng West Road, Fengxian District, Shanghai 201400, China. Electronic address:
Article Synopsis
- Serratia marcescens Nuclease A (SmNucA) is commonly used in biopharmaceutical manufacturing to remove nucleotide impurities, but its effectiveness drops significantly in high-salt environments (up to 500 mM).
- Researchers developed a variant called HighSalt NucA, which has four Lys mutations to enhance its ability to bind nucleic acids under these salty conditions, also revealing a new catalytic mechanism.
- Additional experiments showed that other mutations (involving Arg and various hydrophobic or polar residues) also contribute to salt tolerance, allowing HighSalt NucA to maintain its activity and broaden its application potential in nucleic acid removal processes.
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Department of Biology, University of Naples Federico II, Via Cinthia, 21, 80126, Naples, Italy. Electronic address:
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Epstein-Barr virus (EBV) is a ubiquitous oncogenic virus associated with multiple cancers and autoimmune diseases. Unlike most herpesviruses, EBV reactivation from latency occurs asymptomatically, allowing it to spread efficiently to other hosts. However, available models are limited by the inefficient and asynchronous reactivation from latency into lytic replication.
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