Changes in the Structure of Potato Virus A Virions after Limited in situ Proteolysis According to Tritium Labeling Data and Computer Simulation

Ksenofontov, A.L.; Baratova, L.A.; Semenyuk, P.I.; Fedorova, N.V.; Badun, G.A.

Авторы: Ksenofontov Alexander L., Baratova Ludmila A., Semenyuk Pavel I., Fedorova Natalia V., Badun Gennadii A.
Журнал: Biochemistry (Moscow)
Том: 88
Номер: 12-13
Год издания: 2023
Издательство: Pleiades Publishing, Ltd
Местоположение издательства: Road Town, United Kingdom
Первая страница: 2146
Последняя страница: 2156
DOI: 10.1134/s0006297923120167
Аннотация: Abstract— Coat proteins (CP) of the potato virus A virions (PVA) contain partially disordered N-terminal domains, whichare necessary for performing vital functions of the virus. Comparative analysis of the structures of coat proteins (CPs) inthe intact PVA virions and in the virus particles lacking N-terminal 32 amino acids (PVAΔ32) was carried out in this workbased on the tritium planigraphy data. Using atomic-resolution structure of the potato virus Y potyvirus (PVY) protein,which is a homolog of the CP PVA, the available CP surfaces in the PVY virion were calculated and the areas of intersubunit/interhelix contacts were determined. For this purpose, the approach of Lee and Richards [Lee, B., and Richards,F. M. (1971) J. Mol. Biol., 55, 379-400] was used. Comparison of incorporation profiles of the tritium label in the intactand trypsin-degraded PVAΔ32 revealed position of the ΔN-peptide shielding the surface domain (a.a. 66-73, 141-146) andthe interhelix zone (a.a. 161-175) of the PVA CP. Presence of the channels/cavities was found in the virion, which turnedout to be partially permeable to tritium atoms. Upon removal of the ΔN-peptide, decrease in the label incorporation withinthe virion (a.a. 184-200) was also observed, indicating possible structural transition leading to the virion compactization.Based on the obtained data, we can conclude that part of the surface ΔN-peptide is inserted between the coils of the virionhelix thus increasing the helix pitch and providing greater flexibility of the virion, which is important for intercellular transport of the viruses in the plants.
Добавил в систему: Ксенофонтов Александр Леонидович

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Changes in the Structure of Potato Virus A Virions after Limited in situ Proteolysis According to Tritium Labeling Data and Computer Simulationстатья

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