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Architectural organization and in situ fusion protein structure of lymphocytic choriomeningitis virus

Authors
  • Kang, Joon S.
  • Zhou, Kang
  • Wang, Hui
  • Tang, Sijia
  • Lyles, Kristin Van Mouwerik
  • Luo, Ming
  • Zhou, Z. Hong
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
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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.

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