Abstract:We developed a method for the fast transformation of virions of tobacco mosaic virus (TMV) in so-called spherical particles (SPs) of different sizes. These SPs turned out to be highly useful for the preparation of different kinds of important biotechnological products. In this communication, we report that a representative of the flexuous helical virus group-potato virus X (PVX), produces SPs as well, but these SPs differ from TMV SPs in several important aspects. PVX SPs may be useful biotechnological devices. Show more
“…Furthermore, reaction of SPs with thioflavin T suggests the appearance of cross-β-structures and amyloid-like structures. It is likely that, with the emergence of thermal associations of the TMV coat protein, the newly formed β-structures are involved in interactions between subunits, as we have shown for thermal denaturation of CP potato virus A [34] and potato virus X [35].…”
Previously, we have reported that spherical particles (SPs) are formed by the thermal remodeling of rigid helical virions of native tobacco mosaic virus (TMV) at 94°C. SPs have remarkable features: stability, unique adsorption properties and immunostimulation potential. Here we performed a comparative study of the amino acid composition of the SPs and virions surface to characterize their properties and take an important step to understanding the structure of SPs. The results of tritium planigraphy showed that thermal transformation of TMV leads to a significant increase in tritium label incorporation into the following sites of SPs protein: 41–71 а.a. and 93–122 a.a. At the same time, there was a decrease in tritium label incorporation into the N- and C- terminal region (1–15 a.a., 142–158 a.a). The use of complementary physico-chemical methods allowed us to carry out a detailed structural analysis of the surface and to determine the most likely surface areas of SPs. The obtained data make it possible to consider viral protein thermal rearrangements, and to open new opportunities for biologically active complex design using information about SPs surface amino acid composition and methods of non-specific adsorption and bioconjugation.
“…Furthermore, reaction of SPs with thioflavin T suggests the appearance of cross-β-structures and amyloid-like structures. It is likely that, with the emergence of thermal associations of the TMV coat protein, the newly formed β-structures are involved in interactions between subunits, as we have shown for thermal denaturation of CP potato virus A [34] and potato virus X [35].…”
Previously, we have reported that spherical particles (SPs) are formed by the thermal remodeling of rigid helical virions of native tobacco mosaic virus (TMV) at 94°C. SPs have remarkable features: stability, unique adsorption properties and immunostimulation potential. Here we performed a comparative study of the amino acid composition of the SPs and virions surface to characterize their properties and take an important step to understanding the structure of SPs. The results of tritium planigraphy showed that thermal transformation of TMV leads to a significant increase in tritium label incorporation into the following sites of SPs protein: 41–71 а.a. and 93–122 a.a. At the same time, there was a decrease in tritium label incorporation into the N- and C- terminal region (1–15 a.a., 142–158 a.a). The use of complementary physico-chemical methods allowed us to carry out a detailed structural analysis of the surface and to determine the most likely surface areas of SPs. The obtained data make it possible to consider viral protein thermal rearrangements, and to open new opportunities for biologically active complex design using information about SPs surface amino acid composition and methods of non-specific adsorption and bioconjugation.
“…Isolation of viruses, viral RNA, and coat proteins PVX and TMV samples were isolated according to [6] and [7], respectively; AltMV was isolated according to [8]. RNA was isolated by a modified phenolic method [9].…”
Currently, the assembly of helical plant viruses is poorly understood. The viral assembly and infection may be affected by the charge distribution on the virion surface. However, only the total virion charge (isoelectric point) has been determined for most plant viruses. Here, we report on the first application of positively charged magnetic nanoparticles for mapping the surface charge distribution of helical plant viruses. The charge was demonstrated to be unevenly distributed on the surface of viruses belonging to different taxonomic groups, with the negative charge being predominantly located at one end of the virions. This charge distribution is mainly controlled by viral RNA.
“…When filamentous PVX VLPs are heated to 70 °C they swell, and at 90 °C, spherical VLPs are formed [ 57 ], akin to TMV structures at higher temperatures [ 58 ]. The maximum diameter of spherical PVX particles is 77 nm, these RNA free particles revealed different predicted secondary structures of denatured CP compared to the CP of the filamentous PVX particles [ 59 ].…”
Section: Categories Of Plant Virus Nanoparticlesmentioning
Naturally occurring viral nanomaterials have gained popularity owing to their biocompatible and biodegradable nature. Plant virus nanoparticles (VNPs) can be used as nanocarriers for a number of biomedical applications. Plant VNPs are inexpensive to produce, safe to administer and efficacious as treatments. The following review describes how plant virus architecture facilitates the use of VNPs for imaging and a variety of therapeutic applications, with particular emphasis on cancer. Examples of plant viruses which have been engineered to carry drugs and diagnostic agents for specific types of cancer are provided. The drug delivery system in response to the internal conditions is known as stimuli response, recently becoming more applicable using plant viruses based VNPs. The review concludes with a perspective of the future of plant VNPs and plant virus-like particles (VLPs) in cancer research and therapy.
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