Architectural organization and in situ fusion protein structure of lymphocytic choriomeningitis virus
- Authors
- Type
- Published Article
- Journal
- Journal of Virology
- Publisher
- American Society for Microbiology
- Publication Date
- Sep 27, 2024
- Volume
- 98
- Issue
- 10
- Identifiers
- DOI: 10.1128/jvi.00640-24
- Source
- ASM Journals
- Keywords
- License
- Yellow
Abstract
The impact of COVID-19 on public health has highlighted the importance of understanding zoonotic pathogens. Lymphocytic choriomeningitis virus (LCMV) is a rodent-borne human pathogen that causes hemorrhagic fever. Herein, we describe the in situ structure of LCMV proteins and their architectural organization on the viral envelope and around the nucleocapsid. The virion structure reveals the distribution of the surface glycoprotein complex (GPC) and the contact points between the viral envelope and the underlying matrix protein, as well as the association with the nucleocapsid. The morphology and sizes of virions, as well as the number of RNA polymerase L inside each virion vary greatly, highlighting the fast-changing nature of LCMV. A comparison between the in situ GPC trimeric structure and prior ectodomain structures identifies the transmembrane and endo domains of GPC and key interactions among its subunits. The work provides new insights into LCMV assembly and informs future structure-guided vaccine design.