The role of the 5′-cap structure in viral ribonucleoproteins assembly from potato virus X coat protein and RNAs

Petrova, E.K.; Nikitin, Nikolai A.; Protopopova, Anna D.; Arkhipenko, M. V.; Яминский, И.В.; Карпова, О. В.; Atabekov, J.G.

doi:10.1016/j.biochi.2013.09.004

Cited by 13 publications

(18 citation statements)

References 38 publications

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“…Recently, the PVX assembly was found to be initiated at the 5´ terminus of genomic RNA, where the cap structure is an important condition for virus assembly [30]. Since bacteria are not able to create the cap structure, it is very unlikely that regular VLPs would be formed upon expression in bacteria.…”

Section: Discussionmentioning

confidence: 99%

New positions for peptide presentation in Potato virus X capsid protein

et al. 2015

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viruses represents potentially a promising new delivery and adjuvant system mainly for the following reasons: (i) the capsid of plant virus represents a scaffold exposing desired epitopes to the immune system in an abundant and organized manner and can serve as an adjuvant by itself, (ii) plant viruses are not infectious to animals, lowering the safety risk associated with their deployment, and (iii) scalability [3,4].Human papillomavirus (HPV) infection is one of the most common sexually transmitted infections worldwide. Infection by high risk HPVs is causally associated with cervical cancer, which represents the second most common cancer among women (after breast cancer) [5]. The most common oncogenic HPV genotypes are 16 and 18, together causing approximately 70 % of all cervical cancers, while HPV 16 alone causing 50 % of all cervical cancers [6]. The E7 oncoprotein plays an important role in both malignant transformation and in the maintenance of the transformed state of HPV infected cells. This represents a promising target for immunotherapy because the E7 oncoprotein is expressed in all cervical tumors and in precancerous lesions [7]. The main known role of E7 oncoprotein in virus cycle is to prevent cell death by binding tumor-suppressor protein Rb (pRb), resulting in the dissociation of pRB from E2F-family transcription factors and the premature cell progression into the S phase of the cell cycle which leads to uncontrollable cell division [8].Potato virus X (PVX) belongs to the order Tymovirales, family Alphaflexiviridae and genus Potexvirus. It is a filamentous, positive single stranded RNA (+ssRNA) virus. Virus particles are about 515 nm long and have about 13 nm in diameter. The PVX genome is capped, has a poly(A) tail and encodes five open reading frames (viral replicase, three movement proteins belonging to the triple-gene block family and capsid protein -approximately 1 300 CP subunits per virion) [9]. The PVX CP can be used for presentation by direct or indirect fusion of a desired protein or peptide to the N-terminus [10][11][12]. Recently, it has been also shown that the C-terminus of PVX CP can be used for protein presentation [13]. However, the Abstract: Potato virus X (PVX) is widely used as a peptide presentation system in plant biotechnology, mostly for transient expression of desired peptides fused to the N-terminus of its capsid protein (CP). Here we describe testing/investigation of new positions for peptide presentation based on seven putative surface loops of PVX CP. We performed bacterial expression of fourteen different PVX CPs modified by the insertion of the epitope derived from the E7 oncoprotein (E7 epitope) of Human papillomavirus type 16 fused with His tag. The expression from vector pMPM-A4Ω in Escherichia coli MC1061 was performed to evaluate the capacity of the PVX CP platform to tolerate the insertion of E7 epitope fused with His tag in the seven putative surface loops. The immunological characteristics of expressed epitopes were assessed by Western blot using both anti-P...

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Section: Discussionmentioning

confidence: 99%

New positions for peptide presentation in Potato virus X capsid protein

et al. 2015

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“…Образцы для электронной микроскопии были приготовлены согласно [2,3], анализ проводили с помощью электронного микроскопа JEM-1011 (JEOL, Япония).…”

Section: материалы и методыunclassified

“…Образцы для атомно-силовой микроскопии были приготовлены и проанализированы, как опи-сано ранее [3].…”

Section: материалы и методыunclassified

“…Однако удаление кэп-структуры после предварительного кэпирования РНК в дальнейшем не препятствует образованию вРНП. Было высказано предположение, что кэп-структура не является сигналом сборки сама по себе, но влияет на 5′-конец молекулы РНК, создавая кон-формационный сигнал упаковки и способствуя эффективному взаимодействию РНК и БО ХВК [3,4].…”

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“…Это затрудняет анализ сборки вРНП при инкубации 5′-концевых транс-криптов ВМАльт с БО ВМАльт, поэтому было принято решение исследовать сборку вРНП при инкубации транскриптов с БО ХВК, который не полимеризуется в отсутствие РНК [3,8].…”

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Study of the potexvirus ribonucleoproteins signal of assembly

Petrova

Trifonova

Nikitin

et al. 2016

Moscow Univ. Biol.Sci. Bull.

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3D Puzzle at the Nanoscale–How do RNA Viruses Self‐Assemble their Capsids into Perfectly Ordered Structures

Kordys,

Urbanowicz

2024

Macromolecular Bioscience

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The phenomenon of RNA virus self‐organization, first observed in the mid‐20th century in tobacco mosaic virus, is the subject of extensive research. Efforts to comprehend this process intensify due to its potential for producing vaccines or antiviral compounds as well as nanocarriers and nanotemplates. However, direct observation of the self‐assembly is hindered by its prevalence within infected host cells. One of the approaches involves in vitro and in silico research using model viruses featuring a ssRNA(+) genome enclosed within a capsid made up of a single type protein. While various pathways are proposed based on these studies, their relevance in vivo remains uncertain. On the other hand, the development of advanced microscopic methods provide insights into the events within living cells, where following viral infection, specialized compartments form to facilitate the creation of nascent virions. Intriguingly, a growing body of evidence indicates that the primary function of packaging signals in viral RNA is to effectively initiate the virion self‐assembly. This is in contrast to earlier opinions suggesting a role in marking RNA for encapsidation. Another noteworthy observation is that many viruses undergo self‐assembly within membraneless liquid organelles, which are specifically induced by viral proteins.

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The role of the 5′-cap structure in viral ribonucleoproteins assembly from potato virus X coat protein and RNAs

Cited by 13 publications

References 38 publications

New positions for peptide presentation in Potato virus X capsid protein

New positions for peptide presentation in Potato virus X capsid protein

Study of the potexvirus ribonucleoproteins signal of assembly

3D Puzzle at the Nanoscale–How do RNA Viruses Self‐Assemble their Capsids into Perfectly Ordered Structures

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