Open AccessThermal remodelling of Alternanthera mosaic virus virions and virus-like particles into protein spherical particles
Author(s) -
Tatiana I. Manukhova,
Ekaterina A. Evtushenko,
Alexander L. Ksenofontov,
Alexander M. Arutyunyan,
Angelina Kovalenko,
Nikolai A. Nikitin,
О. В. Карпова
Publication year - 2021
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0255378
Subject(s) - circular dichroism , biophysics , cowpea mosaic virus , chemistry , tobacco mosaic virus , virus , thioflavin , virus like particle , fluorescence , biology , plant virus , biochemistry , virology , recombinant dna , medicine , physics , disease , pathology , alzheimer's disease , quantum mechanics , gene
The present work addresses the thermal remodelling of flexible plant viruses with a helical structure and virus-like particles (VLPs). Here, for the first time, the possibility of filamentous Alternanthera mosaic virus (AltMV) virions’ thermal transition into structurally modified spherical particles (SP) has been demonstrated. The work has established differences in formation conditions of SP from virions (SP V ) and VLPs (SP VLP ) that are in accordance with structural data (on AltMV virions and VLPs). SP originate from AltMV virions through an intermediate stage. However, the same intermediate stage was not detected during AltMV VLPs’ structural remodelling. According to the biochemical analysis, AltMV SP V consist of protein and do not include RNA. The structural characterisation of AltMV SP V/VLP by circular dichroism, intrinsic fluorescence spectroscopy and thioflavin T fluorescence assay has been performed. AltMV SP V/VLP adsorption properties and the availability of chemically reactive surface amino acids have been analysed. The revealed characteristics of AltMV SP V/VLP indicate that they could be applied as protein platforms for target molecules presentation and for the design of functionally active complexes.