The Two-Faced Potato Virus X: From Plant Pathogen to Smart Nanoparticle

Abstract

Potato virus X (PVX) is a single-stranded RNA plant virus, historically investigated in light of the detrimental effects on potato, the world’s fourth most important food commodity. The study of the interactions with cells, and more generally with the plant, both locally and systemically, significantly contributed to unveil the mechanisms underlying gene silencing, fundamental not only in plant virology but also in the study of gene expression regulation. Unraveling the molecular events of PVX infection paved the way for the development of different viral expression vectors and consequential applications in functional genomics and in the biosynthesis of heterologous proteins in plants. Apart from that, the ease of manipulation and the knowledge of the virus structure (particle dimensions, shape and physicochemical features) are inspiring novel applications, mainly focused on nanobiotechnology. This review will lead the reader in this area, spanning from fundamental to applied research, embracing fields from plant pathology to vaccine and drug-targeted delivery, imaging and material sciences. Due to the versatile moods, PVX holds promise to become an interesting nanomaterial, in view to create the widest possible arsenal of new “bio-inspired” devices to face evolving issues in biomedicine and beyond.

Engineering Potato Virus X Particles for a Covalent Protein Based Attachment of Enzymes

“…Due to their programmable, highly organized structure and size, virus based platforms are ideal candidates for diverse applications areas . We have established PVX as new platform for simple and stable linking of target proteins by immobilizing the active T. reesei endoglucanase Cel12A using SpyTag/SpyCatcher technology.…”

“…Due to their programmable, highly organized structure and size, virus based platforms are ideal candidates for diverse applications areas. [77][78][79] We have established PVX as new platform for simple and stable linking of target proteins by immobilizing the active T. reesei endoglucanase Cel12A using SpyTag/SpyCatcher technology. This system overcomes limitations arising from genetic fusions to the PVX CP, including size constraints and inappropriate pI values, because these target proteins fused to the SC can be expressed separately.…”

Resistance to viruses of potato: current status and prospects

“…Несмотря на от носительно слабые симптомы инфекции растений PVX при индивидуальном заражении, его патогенность для картофеля особенно сильно проявляется при совместной инфекции с неродственными вирусами, как правило, с представителями рода потивирусов. Наблюдаемый в этих случаях синергизм приводит к значительно большему накоплению каждого отдельного вируса в растениях и развитию сильных симптомов инфекции, что влечет за собой серьезные потери урожая (Aguilar et al, 2015;Lico et al, 2015). Для PVX не обнаружены насекомыепере носчики, он распространяется только механическим путем через сельскохозяйственные орудия при обработке полей и сборе урожая (Lico et al, 2015).…”

“…Наблюдаемый в этих случаях синергизм приводит к значительно большему накоплению каждого отдельного вируса в растениях и развитию сильных симптомов инфекции, что влечет за собой серьезные потери урожая (Aguilar et al, 2015;Lico et al, 2015). Для PVX не обнаружены насекомыепере носчики, он распространяется только механическим путем через сельскохозяйственные орудия при обработке полей и сборе урожая (Lico et al, 2015). Вирус PVМ входит в состав рода Carlavirus семейства Betaflexiviridae.…”

Metabolic engineering of plants using a disarmed potyvirus vector

“…This vector was further improved when the translation enhancer of the Alfalfa mosaic virus (AMV) RNA4 was added (Mardanova et al, 2009) (Figure 2B). Beside gene expression systems, PVX VNPs and VLPS were also used for imaging, drug delivery and diagnosis (Lico et al, 2015). Peptides can be fused directly to the CP or by inserting the 2A sequence of the Foot-and-mouth disease virus between the capsid protein and the GOI, enabling presentation of larger proteins on the capsid's surface.…”