Name
Comparative Cryo-EM Analysis of Rotavirus Virus-Like Particles Across Phylogenetic Clades Reveals Structural Determinants of Assembly and Evolution
Presenter
Daniel Luque, The University of New South Wales
Co-Author(s)
Dunia Asensio-Cob1, Javier M. Rodríguez2, Daniel Luque3,4
1 Department of Molecular Medicine, Peter Gilgan Centre for Research and Learning, The Hospital for Sick Children, 686 Bay Street, Toronto ON, M5G0A4, Canada.
2 Departamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología, CSIC, Cantoblanco, 28049 Madrid, Spain.
3Electron Microscope Unit, Mark Wainwright Analytical Centre, University of New South Wales, Sydney, NSW 2052, Australia.
4 School of Biomedical Sciences, University of New South Wales, Sydney, NSW 2052, Australia.
Abstract Category
Structural Biology
Abstract
Rotaviruses (RVs) are a major cause of gastroenteritis and dehydration in children under five, responsible for 590 million infections annually. RVs are classified into ten species (A–J), with RVA, RVB, RVC, and RVH infecting humans. Due to the limited ability to cultivate non-RVA species, structural characterization of these viruses has remained a challenge. To overcome this limitation, recombinant baculovirus-based expression systems have been used to produce double-layered virus-like particles (vDLPs), enabling structural comparisons across RV species.
Here, we present the high-resolution cryo-electron microscopy (cryo-EM) structures of RVA, RVD, and RVI vDLPs, providing new insights into rotavirus assembly and evolutionary divergence. RVA and RVD, belonging to the same phylogenetic clade, exhibit a high degree of conservation in VP2 and VP6, with minor differences localized to intermonomer contact loops. In contrast, RVI, from a distinct clade, shows substantial structural divergence throughout both proteins, suggesting functional adaptations influencing host tropism and capsid stability.
Here, we present the high-resolution cryo-electron microscopy (cryo-EM) structures of RVA, RVD, and RVI vDLPs, providing new insights into rotavirus assembly and evolutionary divergence. RVA and RVD, belonging to the same phylogenetic clade, exhibit a high degree of conservation in VP2 and VP6, with minor differences localized to intermonomer contact loops. In contrast, RVI, from a distinct clade, shows substantial structural divergence throughout both proteins, suggesting functional adaptations influencing host tropism and capsid stability.