ArticleViruses2024
Structural Heterogeneity of the Rabies Virus Virion.
Article in Viruses, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- Rabies Virus Glycoprotein G Variation Is Associated with Neurovirulence and Reduced Vamp2 Abundance in a Mouse Model of Direct CNS Infection.Veterinary sciences · 2026Article
- Assembly of the Linear Viral Nucleocapsid.Microorganisms · 2026Article
- Advantages and Limitations of AlphaFold in Structural Biology: Insights from Recent Studies.The protein journal · 2026Review
- A Rabies Virus Nucleocapsid-like Nanostructure Vaccine Based on Dual-Cationic Lipid Nanoparticles.Vaccines · 2025Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Rabies virus (RABV) is among the first recognized viruses of public health concern and has historically contributed to the development of viral vaccines. Despite these significances, the three-dimensional structure of the RABV virion remains unknown due to the challenges in isolating structurally homogenous virion samples in sufficient quantities needed for structural investigation. Here, by combining the capabilities of cryogenic electron tomography (cryoET) and microscopy (cryoEM), we determined the three-dimensional structure of the wild-type RABV virion. Tomograms of RABV virions reveal a high level of structural heterogeneity among the bullet-shaped virion particles encompassing the glycoprotein (G) trimer-decorated envelope and the nucleocapsid composed of RNA, nucleoprotein (N), and matrix protein (M). The structure of the trunk region of the virion was determined by cryoEM helical reconstruction, revealing a one-start N-RNA helix bound by a single layer of M proteins at an N:M ratio of 1. The N-M interaction differs from that in fellow rhabdovirus vesicular stomatitis virus (VSV), which features two layers of M stabilizing the N-RNA helix at an M:N ratio of 2. These differences in both M-N stoichiometry and binding allow RABV to flex its N-RNA helix more freely and point to different mechanisms of viral assembly between these two bullet-shaped rhabdoviruses.
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Registered trials
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