Advanced computational studies, including molecular dynamics, have revealed the need to maintain intrinsically disordered regions of a functionalized coat protein, in order to obtain assembled viral nanoparticles.
The functionalization process of the turnip mosaic virus coat protein (CP) allows to obtain derived viral nanoparticles (VNPs) with multiple biotechnological applications. However, certain functionalizations interfere in the VNP assembly, and no obvious characteristics of the protein sequences inserted in the CP allow an ‘a priori’ identification of the interfering ones. Now, CBGP researchers provide, for the first time, a dynamic view of the complete CP by means of sophisticated computational studies, including the description of the necessary intrinsic disorder in the N-terminal region where functionalizations take place. Preserving this intrinsic disorder, which allows the interaction of a subdomain of the region with the ordered central region of the CP, is an absolute requisite for assembly. This finding allows the rationalization of the design process of new functionalized VNPs.
Mínguez-Toral, M., Pacios, L.F., Sánchez, F., Ponz, F. 2023. Structural intrinsic disorder in a functionalized potyviral coat protein as a main viability determinant of its assembled nanoparticles. International Journal of Biological Macromolecules 236, 123958. DOI: 10.1016/j.ijbiomac.2023.123958