Research output: Contribution to journal › Review article › peer-review
Research output: Contribution to journal › Review article › peer-review
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TY - JOUR
T1 - Structural Insights into Plant Viruses Revealed by Small-Angle X-ray Scattering and Atomic Force Microscopy
AU - Shtykova, Eleonora V.
AU - Dubrovin, Evgeniy V.
AU - Ksenofontov, Alexander L.
AU - Gifer, Polina K.
AU - Petoukhov, Maxim V.
AU - Tokhtar, Valeriy K.
AU - Sapozhnikova, Irina M.
AU - Stavrianidi, Andrey N.
AU - Kordyukova, Larisa V.
AU - Batishchev, Oleg V.
N1 - OVB was supported by the Russian Science Foundation (grant No. 22-13-00435); PKG was supported by the project “UMNIK-MIPT-2021”, contract no. 17386GU/2022; VKT was supported by the by the grant of the Ministry of Science and Higher Education of the Russian Federation No. FZWG-2023-0007; IMS was supported by the Ministry of Science and Higher Education of the Russian Federation (Ural Federal University Program of Development within the Priority-2030 Program, agreement No. 075-15-2023-373 from 20 February 2023). The work was carried out within the state assignment of NRC “Kurchatov Institute”.
PY - 2024
Y1 - 2024
N2 - The structural study of plant viruses is of great importance to reduce the damage caused by these agricultural pathogens and to support their biotechnological applications. Nowadays, X-ray crystallography, NMR spectroscopy and cryo-electron microscopy are well accepted methods to obtain the 3D protein structure with the best resolution. However, for large and complex supramolecular structures such as plant viruses, especially flexible filamentous ones, there are a number of technical limitations to resolving their native structure in solution. In addition, they do not allow us to obtain structural information about dynamics and interactions with physiological partners. For these purposes, small-angle X-ray scattering (SAXS) and atomic force microscopy (AFM) are well established. In this review, we have outlined the main principles of these two methods and demonstrated their advantages for structural studies of plant viruses of different shapes with relatively high spatial resolution. In addition, we have demonstrated the ability of AFM to obtain information on the mechanical properties of the virus particles that are inaccessible to other experimental techniques. We believe that these under-appreciated approaches, especially when used in combination, are valuable tools for studying a wide variety of helical plant viruses, many of which cannot be resolved by classical structural methods.
AB - The structural study of plant viruses is of great importance to reduce the damage caused by these agricultural pathogens and to support their biotechnological applications. Nowadays, X-ray crystallography, NMR spectroscopy and cryo-electron microscopy are well accepted methods to obtain the 3D protein structure with the best resolution. However, for large and complex supramolecular structures such as plant viruses, especially flexible filamentous ones, there are a number of technical limitations to resolving their native structure in solution. In addition, they do not allow us to obtain structural information about dynamics and interactions with physiological partners. For these purposes, small-angle X-ray scattering (SAXS) and atomic force microscopy (AFM) are well established. In this review, we have outlined the main principles of these two methods and demonstrated their advantages for structural studies of plant viruses of different shapes with relatively high spatial resolution. In addition, we have demonstrated the ability of AFM to obtain information on the mechanical properties of the virus particles that are inaccessible to other experimental techniques. We believe that these under-appreciated approaches, especially when used in combination, are valuable tools for studying a wide variety of helical plant viruses, many of which cannot be resolved by classical structural methods.
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U2 - 10.3390/v16030427
DO - 10.3390/v16030427
M3 - Review article
VL - 16
JO - Viruses
JF - Viruses
SN - 1999-4915
IS - 3
M1 - 427
ER -
ID: 55351173