Structural Heterogeneity of the Rabies Virus Virion. Cai, X., Zhou, K., Alvarez-Cabrera, A. L., Si, Z., Wang, H., He, Y., Li, C., & Zhou, Z. H. Viruses, 16(9):1447, Multidisciplinary Digital Publishing Institute, September, 2024. doi abstract bibtex 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.
@article{caiStructuralHeterogeneityRabies2024,
title = {Structural {{Heterogeneity}} of the {{Rabies Virus Virion}}},
author = {Cai, Xiaoying and Zhou, Kang and {Alvarez-Cabrera}, Ana Lucia and Si, Zhu and Wang, Hui and He, Yao and Li, Cally and Zhou, Z. Hong},
year = {2024},
month = sep,
journal = {Viruses},
volume = {16},
number = {9},
pages = {1447},
publisher = {Multidisciplinary Digital Publishing Institute},
issn = {1999-4915},
doi = {10.3390/v16091447},
urldate = {2025-04-04},
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.},
copyright = {http://creativecommons.org/licenses/by/3.0/},
langid = {english},
keywords = {cryogenic electron microscopy,cryogenic electron tomography,dynamics,flexibility,rabies virus,rhabdoviruses,wild type},
file = {C:\Users\shervinnia\Zotero\storage\DV59DN8Z\Cai et al. - 2024 - Structural Heterogeneity of the Rabies Virus Virion.pdf}
}
Downloads: 0
{"_id":"FfcXSRMbAjZLZ3SER","bibbaseid":"cai-zhou-alvarezcabrera-si-wang-he-li-zhou-structuralheterogeneityoftherabiesvirusvirion-2024","author_short":["Cai, X.","Zhou, K.","Alvarez-Cabrera, A. L.","Si, Z.","Wang, H.","He, Y.","Li, C.","Zhou, Z. H."],"bibdata":{"bibtype":"article","type":"article","title":"Structural Heterogeneity of the Rabies Virus Virion","author":[{"propositions":[],"lastnames":["Cai"],"firstnames":["Xiaoying"],"suffixes":[]},{"propositions":[],"lastnames":["Zhou"],"firstnames":["Kang"],"suffixes":[]},{"propositions":[],"lastnames":["Alvarez-Cabrera"],"firstnames":["Ana","Lucia"],"suffixes":[]},{"propositions":[],"lastnames":["Si"],"firstnames":["Zhu"],"suffixes":[]},{"propositions":[],"lastnames":["Wang"],"firstnames":["Hui"],"suffixes":[]},{"propositions":[],"lastnames":["He"],"firstnames":["Yao"],"suffixes":[]},{"propositions":[],"lastnames":["Li"],"firstnames":["Cally"],"suffixes":[]},{"propositions":[],"lastnames":["Zhou"],"firstnames":["Z.","Hong"],"suffixes":[]}],"year":"2024","month":"September","journal":"Viruses","volume":"16","number":"9","pages":"1447","publisher":"Multidisciplinary Digital Publishing Institute","issn":"1999-4915","doi":"10.3390/v16091447","urldate":"2025-04-04","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.","copyright":"http://creativecommons.org/licenses/by/3.0/","langid":"english","keywords":"cryogenic electron microscopy,cryogenic electron tomography,dynamics,flexibility,rabies virus,rhabdoviruses,wild type","file":"C:\\Users\\shervinnia\\Zotero\\storage\\DV59DN8Z\\Cai et al. - 2024 - Structural Heterogeneity of the Rabies Virus Virion.pdf","bibtex":"@article{caiStructuralHeterogeneityRabies2024,\n title = {Structural {{Heterogeneity}} of the {{Rabies Virus Virion}}},\n author = {Cai, Xiaoying and Zhou, Kang and {Alvarez-Cabrera}, Ana Lucia and Si, Zhu and Wang, Hui and He, Yao and Li, Cally and Zhou, Z. Hong},\n year = {2024},\n month = sep,\n journal = {Viruses},\n volume = {16},\n number = {9},\n pages = {1447},\n publisher = {Multidisciplinary Digital Publishing Institute},\n issn = {1999-4915},\n doi = {10.3390/v16091447},\n urldate = {2025-04-04},\n 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.},\n copyright = {http://creativecommons.org/licenses/by/3.0/},\n langid = {english},\n keywords = {cryogenic electron microscopy,cryogenic electron tomography,dynamics,flexibility,rabies virus,rhabdoviruses,wild type},\n file = {C:\\Users\\shervinnia\\Zotero\\storage\\DV59DN8Z\\Cai et al. - 2024 - Structural Heterogeneity of the Rabies Virus Virion.pdf}\n}\n\n","author_short":["Cai, X.","Zhou, K.","Alvarez-Cabrera, A. L.","Si, Z.","Wang, H.","He, Y.","Li, C.","Zhou, Z. H."],"key":"caiStructuralHeterogeneityRabies2024","id":"caiStructuralHeterogeneityRabies2024","bibbaseid":"cai-zhou-alvarezcabrera-si-wang-he-li-zhou-structuralheterogeneityoftherabiesvirusvirion-2024","role":"author","urls":{},"keyword":["cryogenic electron microscopy","cryogenic electron tomography","dynamics","flexibility","rabies virus","rhabdoviruses","wild type"],"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bibbase.org/network/files/2MtabhipmJFGQ7n9n","dataSources":["mrv2RSxFMmgGBMu4y"],"keywords":["cryogenic electron microscopy","cryogenic electron tomography","dynamics","flexibility","rabies virus","rhabdoviruses","wild type"],"search_terms":["structural","heterogeneity","rabies","virus","virion","cai","zhou","alvarez-cabrera","si","wang","he","li","zhou"],"title":"Structural Heterogeneity of the Rabies Virus Virion","year":2024}