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Effect of the Coat Protein N-Terminal Domain Structure on the Structure and Physicochemical Properties of Virions of Potato Virus X and Alternanthera Mosaic Virusстатья
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 26 июня 2024 г.
- Авторы: Ksenofontov Alexander L., Petoukhov Maxim V., Matveev Vladimir V., Fedorova N.V., Semenyuk Pavel I., Arutyunyan Alexander M., Manukhova Tatiana I., Evtushenko Ekaterina A., Nikitin Nikolai A., Karpova Olga V., Shtykova Eleonora V.
- Журнал: Biochemistry (Moscow)
- Том: 88
- Номер: 1
- Год издания: 2023
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 119
- Последняя страница: 130
- DOI: 10.1134/s0006297923010108
- Аннотация: The amino acid sequences of the coat proteins (CPs) of the potexviruses potato virus X (PVX) and alternanthera mosaic virus (AltMV) share ~40% identity. The N-terminal domains of these proteins differ in the amino acid sequence and the presence of the N-terminal fragment of 28 residues (ΔN peptide) in the PVX CP. Here, we determined the effect of the N-terminal domain on the structure and physicochemical properties of PVX and AltMV virions. The circular dichroism spectra of these viruses differed significantly, and the melting point of PVX virions was 10-12°C higher than that of AltMV virions. Alignment of the existing high-resolution 3D structures of the potexviral CPs showed that the RMSD value between the C α -atoms was the largest for the N-terminal domains of the two compared models. Based on the computermodeling, the ΔN peptide of the PVX CP is fully disordered. According to the synchrotron small-angle X-ray scattering(SAXS) data, the structure of CPs from the PVX and AltMV virions differ; in particular, the PVX CP has a larger portion of crystalline regions and, therefore, is more ordered. Based on the SAXS data, the diameters of the PVX and AltMV virionsand helix parameters in solution were calculated. The influence of the conformation of the PVX CP N-terminal domain and its position relative to the virion surface on the virion structure was investigated. Presumably, an increased thermalstability of PVX virions vs. AltMV is provided by the extended N-terminal domain (ΔN peptide, 28 amino acid residues), which forms additional contacts between the adjacent CP subunits in the PVX virion.
- Добавил в систему: Ксенофонтов Александр Леонидович