AI Article Synopsis
- The rabies virus (RABV) has historical importance in public health and vaccine development, but its 3D structure has been unclear due to difficulties in isolating consistent samples.
- Researchers utilized advanced techniques like cryogenic electron tomography and microscopy to determine the RABV virion's 3D structure, revealing structural diversity among its bullet-shaped particles.
- The study found that the interaction between nucleoprotein (N) and matrix protein (M) in RABV differs from that in a related virus (VSV), affecting the flexibility of the N-RNA helix and suggesting distinct viral assembly mechanisms.
Article 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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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11437398 | PMC |
| http://dx.doi.org/10.3390/v16091447 | DOI Listing |
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- The rabies virus (RABV) has historical importance in public health and vaccine development, but its 3D structure has been unclear due to difficulties in isolating consistent samples.
- Researchers utilized advanced techniques like cryogenic electron tomography and microscopy to determine the RABV virion's 3D structure, revealing structural diversity among its bullet-shaped particles.
- The study found that the interaction between nucleoprotein (N) and matrix protein (M) in RABV differs from that in a related virus (VSV), affecting the flexibility of the N-RNA helix and suggesting distinct viral assembly mechanisms.
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