The Melolontha melolontha entomopoxvirus fusolin protein is a chitin-active lytic polysaccharide monooxygenase that displays extreme stability.

Abstract

Spindles are intracellular crystals of the fusolin protein that enhances 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 was fusolin active after long-term storage, but it also withstood high temperature and oxidative stress in its crystalline form, highlighting extreme stability that is beneficial to viral persistence and desirable for potential biotechnology applications.