The Melolontha melolontha entomopoxvirus fusolin protein is a chitin-active lytic polysaccharide monooxygenase that displays extreme stability.
Jennifer Sarah Maria LooseMarion BoudesMax BergoinFasséli CoulibalyGustav Vaaje-KolstadPublished in: FEBS letters (2023)
Spindles are intracellular crystals of the fusolin protein that enhance the oral virulence of insect poxviruses by disruption of the larval chitinous peritrophic matrix. The enigmatic fusolin protein is classified as a lytic polysaccharide monooxygenase (LPMO) by sequence and structure. Although circumstantial evidence points towards a role for fusolin in chitin degradation, no biochemical data exist to verify this claim. In the present study we demonstrate that fusolin released from over 40-year-old spindles, stored for 10 years at 4 °C, are chitin-degrading LPMOs. Not only were the fusolins active after long-term storage, but, in its crystalline form, fusolin also withstood high temperature and oxidative stress, highlighting an extreme stability that is beneficial to viral persistence and desirable for potential biotechnology applications.
Keyphrases
- oxidative stress
- high temperature
- room temperature
- protein protein
- amino acid
- climate change
- binding protein
- escherichia coli
- pseudomonas aeruginosa
- dna damage
- sars cov
- signaling pathway
- biofilm formation
- zika virus
- antimicrobial resistance
- small molecule
- big data
- ischemia reperfusion injury
- deep learning
- cystic fibrosis
- risk assessment
- endoplasmic reticulum stress