bioRxiv Science⌕ Search

bioRxiv · 10.1101/120063

Towards Water-Free Biobanks: Long-Term Dry-Preservation At Room Temperature Of Desiccation-Sensitive Enzyme Luciferase In Air-Dried Insect Cells

Abstract

Desiccation-tolerant cultured cells Pv11 derived from the anhydrobiotic Polypedilum vanderplanki embryo endure complete desiccation because of their ametabolic state and resume their metabolism after rehydration. These features led us to develop a novel dry preservation technology for enzymes as it was still unclear whether Pv11 cells preserved an exogenous enzyme in the dry state. This study shows that Pv11 cells protect an exogenous desiccation-sensitive enzyme, luciferase, preserving the enzymatic activity even after dry storage for 372 days at room temperature. A process including pre-incubation with trehalose, dehydration, storage, and rehydration allowed Pv11 (Pvll-Luc) cells stably expressing luciferase to survive desiccation and still emit luminescence caused by luciferase after rehydration. Luminescence produced by luciferase in Pvll-Luc cells after rehydration did not significantly decrease in presence of a translation inhibitor, showing that the activity did not derive from de novo enzyme synthesis following the resumption of cell metabolism. These findings indicate that the surviving Pv11 cells almost completely protect luciferase during desiccation. Lacking of the preincubation step resulted in the loss of luciferase activity after rehydration. We showed that preincubation with trehalose associated to induction of desiccation-tolerant related genes in Pv11 cells allowed effective in vivo preservation of enzymes in the dry state.

Source connections

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Kikuta, S., Watanabe, S. J., Sato, R., Gusev, O., Nesmelov, A., Sogame, Y., Cornette, R., Kikawada, T.. 2017-03-24. Towards Water-Free Biobanks: Long-Term Dry-Preservation At Room Temperature Of Desiccation-Sensitive Enzyme Luciferase In Air-Dried Insect Cells. https://doi.org/10.1101/120063

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Structure of influenza D virus NS1 reveals a novel Zn-binding site and ssRNA-binding activity

Influenza D virus (IDV) is an emerging pathogen associated with bovine respiratory disease and has potential for zoonotic transmission. Although nonstructural protein 1 (NS1) is a major virulence factor in influenza A and B viruses, the structure and function of IDV NS1 remain poorly defined. Here, we determined crystal structures of the IDV NS1 N-terminal RNA-binding domain (NTD) and C-terminal effector domain (CTD). The NTD retains the conserved homodimeric six-helix fold, whereas the CTD adopts a distinct architecture containing a novel Zn2+-binding site. IDV NS1 CTD preferentially binds single-stranded RNA, and mutagenesis identified lysine and arginine residues critical for this activity. Single-residue substitutions disrupting either the Zn2+-binding site or RNA-binding interface prevented recovery of infectious recombinant IDV. These findings reveal distinct structural and functional features of IDV NS1 and establish the importance of CTD integrity for viral replication. Conservation of key CTD residues in influenza C virus NS1 suggests shared structural features that distinguish influenza C and D virus NS1 proteins from their influenza A and B counterparts.

biochemistry↗

QC-espresso: Brewing quality in proteomics

Data-independent acquisition (DIA) proteomics has become a standard approach for high-throughput proteomics, with DIA-NN emerging as one of the most widely adopted data-analysis platforms. However, despite the detailed information available in DIA-NN output reports, proteomics researchers may lack a streamlined and reproducible approach for assessing acquisition quality, identification consistency, and quantitative reliability across experiments. QC-espresso addresses this need through an automated, report-centered quality-control workflow implemented in R and Quarto. The tool processes a DIA-NN report.parquet file together with the corresponding FASTA database and generates a structured HTML report containing plots, run-level statistics, and exportable summary tables. Application to three experimental datasets allowed the visualization of lower identification depth related to high contaminant content; a chromatographic transition accompanied by altered retention-time and peak-width behavior; and the co-occurrence of systematic mass-error bias with changes in precursor- and protein-level quantitative-quality metrics. QC-espresso can be executed directly in R or through a portable Windows distribution with a graphical launcher, with both modes using the same analytical modules and report-generation workflow. The resulting report provides a consistent record for local inspection and troubleshooting of quality-control metrics within individual DIA proteomics experiments. QC-espresso is freely available at https://github.com/lanfredig/QC-espresso_DIA.

biochemistry↗

Molecular crowding differentially regulates magnetic field-dependent fluorescence, recovery kinetics, and photostability of the magnetosensitive protein MagLOV2

Macromolecular crowding and solvent composition can alter protein conformation, diffusion, hydration, and cofactor photophysics, yet their influence on magnetically sensitive flavoproteins is poorly understood. We tested seven molecular environments in MagLOV2-overexpressing Escherichia coli lysate using a custom-built, high-intensity magnetofluorescence platform. Five-point concentration series of Dextran 70, Ficoll PM70, PEG6000, PEG3350, glycerol, ethylene glycol, and bovine serum albumin (BSA) were measured at 22 mT under continuous 6.12 W/cm2 blue-light excitation. Dextran 70, Ficoll PM70, and PEG6000 progressively attenuated the negative magnetic field effect (MFE), whereas PEG3350 shifted toward mild enhancement at higher concentrations. Glycerol and ethylene glycol enhanced the negative MFE despite producing the strongest slowing of recovery upon the field being switched off (OFF-recovery), while BSA modestly enhanced MFE and accelerated OFF-recovery. Across 105 treatment cuvettes, the change in MFE was not globally correlated with changes in the OFF-recovery time constant (r = -0.07, p = 0.449). The initial pre-field illumination period revealed a second phenotype: Dextran and Ficoll increased late fluorescence loss, whereas glycerol and BSA were photoprotective. Pre-field fluorescence loss correlated moderately with MFE change across the full dataset (r = 0.474, p = 3.28 x 10-7) but not consistently within crowder classes. These findings show that MagLOV2 spin-dependent magnetofluorescence is shaped by crowder chemistry, polymer size, solvent environment, recovery kinetics, and photostability rather than by a single generic crowding or viscosity mechanism.

biochemistry↗