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Academic literature on the topic 'Potyviral Encoded Proteins'
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Journal articles on the topic "Potyviral Encoded Proteins"
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Sabharwal, Pallavi, and Handanahal S. Savithri. "Functional Characterization of Pepper Vein Banding Virus-Encoded Proteins and Their Interactions: Implications in Potyvirus Infection." Viruses 12, no. 9 (September 17, 2020): 1037. http://dx.doi.org/10.3390/v12091037.
Full textAbstract:
Pepper vein banding virus (PVBV) is a distinct species in the Potyvirus genus which infects economically important plants in several parts of India. Like other potyviruses, PVBV encodes multifunctional proteins, with several interaction partners, having implications at different stages of the potyviral infection. In this review, we summarize the functional characterization of different PVBV-encoded proteins with an emphasis on their interaction partners governing the multifunctionality of potyviral proteins. Intrinsically disordered domains/regions of these proteins play an important role in their interactions with other proteins. Deciphering the function of PVBV-encoded proteins and their interactions with cognitive partners will help in understanding the putative mechanisms by which the potyviral proteins are regulated at different stages of the viral life-cycle. This review also discusses PVBV virus-like particles (VLPs) and their potential applications in nanotechnology. Further, virus-like nanoparticle-cell interactions and intracellular fate of PVBV VLPs are also discussed.
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Guo, Deyin, Carl Spetz, Mart Saarma, and Jari P. T. Valkonen. "Two Potato Proteins, Including a Novel RING Finger Protein (HIP1), Interact with the Potyviral Multifunctional Protein HCpro." Molecular Plant-Microbe Interactions® 16, no. 5 (May 2003): 405–10. http://dx.doi.org/10.1094/mpmi.2003.16.5.405.
Full textAbstract:
Potyviral helper-component proteinase (HCpro) is a multifunctional protein exerting its cellular functions in interaction with putative host proteins. In this study, cellular protein partners of the HCpro encoded by Potato virus A (PVA) (genus Potyvirus) were screened in a potato leaf cDNA library using a yeast two-hybrid system. Two cellular proteins were obtained that interact specifically with PVA HCpro in yeast and in the two in vitro binding assays used. Both proteins are encoded by single-copy genes in the potato genome. Analysis of the deduced amino acid sequences revealed that one (HIP1) of the two HCpro interactors is a novel RING finger protein. The sequence of the other protein (HIP2) showed no resemblance to the protein sequences available from databanks and has known biological functions.
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Solovyev, Andrey G., Anastasia K. Atabekova, Alexander A. Lezzhov, Anna D. Solovieva, Denis A. Chergintsev, and Sergey Y. Morozov. "Distinct Mechanisms of Endomembrane Reorganization Determine Dissimilar Transport Pathways in Plant RNA Viruses." Plants 11, no. 18 (September 15, 2022): 2403. http://dx.doi.org/10.3390/plants11182403.
Full textAbstract:
Plant viruses exploit the endomembrane system of infected cells for their replication and cell-to-cell transport. The replication of viral RNA genomes occurs in the cytoplasm in association with reorganized endomembrane compartments induced by virus-encoded proteins and is coupled with the virus intercellular transport via plasmodesmata that connect neighboring cells in plant tissues. The transport of virus genomes to and through plasmodesmata requires virus-encoded movement proteins (MPs). Distantly related plant viruses encode different MP sets, or virus transport systems, which vary in the number of MPs and their properties, suggesting their functional differences. Here, we discuss two distinct virus transport pathways based on either the modification of the endoplasmic reticulum tubules or the formation of motile vesicles detached from the endoplasmic reticulum and targeted to endosomes. The viruses with the movement proteins encoded by the triple gene block exemplify the first, and the potyviral system is the example of the second type. These transport systems use unrelated mechanisms of endomembrane reorganization. We emphasize that the mode of virus interaction with cell endomembranes determines the mechanism of plant virus cell-to-cell transport.
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Genovés, A., J. A. Navarro, and V. Pallás. "Functional analysis of the five melon necrotic spot virus genome-encoded proteins." Journal of General Virology 87, no. 8 (August 1, 2006): 2371–80. http://dx.doi.org/10.1099/vir.0.81793-0.
Full textAbstract:
Function of the melon necrotic spot virus (MNSV) genome-encoded proteins (p29, p89, p7A, p7B and p42) has been studied. Protein-expression mutants of an infectious, full-length cDNA clone of a Spanish MNSV-Al isolate and a recombinant green fluorescent protein (GFP)-expressing virus were used in infection bioassays on melon plants. Results revealed that p29 and p89 are both essential for virus replication, whereas small proteins p7A and p7B are sufficient to support viral movement between adjacent cells operating in trans. It is also demonstrated that, in addition to its structural role as coat protein, p42 is an important factor controlling symptoms and is required for systemic transport. Moreover, both p42 and p7B, among all of the MNSV-encoded proteins, were able to delay RNA silencing in transient-expression assays on GFP-transgenic Nicotiana benthamiana plants. Finally, the presence of p42 also produced an enhancing effect on local spread similar to that of potyviral helper component proteinase (HC-Pro), probably due to its RNA silencing-suppression ability.
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Merits, Andres, Minna-Liisa Rajamäki, Päivi Lindholm, Pia Runeberg-Roos, Tuija Kekarainen, Pietri Puustinen, Katri Mäkeläinen, Jari P. T. Valkonen, and Mart Saarma. "Proteolytic processing of potyviral proteins and polyprotein processing intermediates in insect and plant cells." Journal of General Virology 83, no. 5 (May 1, 2002): 1211–21. http://dx.doi.org/10.1099/0022-1317-83-5-1211.
Full textAbstract:
Processing of the polyprotein encoded by Potato virus A (PVA; genus Potyvirus) was studied using expression of the complete PVA polyprotein or its mutants from recombinant baculoviruses in insect cells. The time-course of polyprotein processing by the main viral proteinase (NIaPro) was examined with the pulse–chase method. The sites at the P3/6K1, CI-6K2 and VPg/NIaPro junctions were processed slowly, in contrast to other proteolytic cleavage sites which were processed at a high rate. The CI-6K2 polyprotein was observed in the baculovirus system and in infected plant cells. In both cell types the majority of CI-6K2 was found in the membrane fraction, in contrast to fully processed CI. Deletion of the genomic region encoding the 6K1 protein prevented proper proteolytic separation of P3 from CI, but did not affect processing of VPg, NIaPro, NIb or CP from the polyprotein. The 6K2-encoding sequence could be removed without any detectable effect on polyprotein processing. However, deletion of either the 6K1 or 6K2 protein-encoding regions rendered PVA non-infectious. Mutations at the 6K2/VPg cleavage site reduced virus infectivity in plants, but had a less pronounced, albeit detectable, effect on proteolytic processing in the baculovirus system. The results of this study indicate that NIaPro catalyses proteolytic cleavages preferentially in cis, and that the 6K1/CI and NIb/CP sites can also be processed in trans. Both 6K peptides are indispensable for virus replication, and proteolytic separation of the 6K2 protein from the adjacent proteins by NIaPro is important for the rate of virus replication and movement.
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Nunna, Haritha, Feng Qu, and Satyanarayana Tatineni. "P3 and NIa-Pro of Turnip Mosaic Virus Are Independent Elicitors of Superinfection Exclusion." Viruses 15, no. 7 (June 28, 2023): 1459. http://dx.doi.org/10.3390/v15071459.
Full textAbstract:
Superinfection exclusion (SIE) is an antagonistic interaction between identical or closely related viruses in host cells. Previous studies by us and others led to the hypothesis that SIE was elicited by one or more proteins encoded in the genomes of primary viruses. Here, we tested this hypothesis using Turnip mosaic virus (TuMV), a member of the genus Potyvirus of the family Potyviridae, with significant economic consequences. To this end, individual TuMV-encoded proteins were transiently expressed in the cells of Nicotiana benthamiana leaves, followed by challenging them with a modified TuMV expressing the green fluorescent protein (TuMV-GFP). Three days after TuMV-GFP delivery, these cells were examined for the replication-dependent expression of GFP. Cells expressing TuMV P1, HC-Pro, 6K1, CI, 6K2, NIa-VPg, NIb, or CP proteins permitted an efficient expression of GFP, suggesting that these proteins failed to block the replication of a superinfecting TuMV-GFP. By contrast, N. benthamiana cells expressing TuMV P3 or NIa-Pro did not express visible GFP fluorescence, suggesting that both of them could elicit potent SIE against TuMV-GFP. The SIE elicitor activity of P3 and NIa-Pro was further confirmed by their heterologous expression from a different potyvirus, potato virus A (PVA). Plants systemically infected with PVA variants expressing TuMV P3 or NIa-Pro blocked subsequent infection by TuMV-GFP. A +1-frameshift mutation in P3 and NIa-Pro cistrons facilitated superinfection by TuMV-GFP, suggesting that the P3 and NIa-Pro proteins, but not the RNA, are involved in SIE activity. Additionally, deletion mutagenesis identified P3 amino acids 3 to 200 of 352 and NIa-Pro amino acids 3 to 40 and 181 to 242 of 242 as essential for SIE elicitation. Collectively, our study demonstrates that TuMV encodes two spatially separated proteins that act independently to exert SIE on superinfecting TuMV. These results lay the foundation for further mechanistic interrogations of SIE in this virus.
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Cui, Hongguang, and Aiming Wang. "Plum Pox Virus6K1 Protein Is Required for Viral Replication and Targets the Viral Replication Complex at the Early Stage of Infection." Journal of Virology 90, no. 10 (March 9, 2016): 5119–31. http://dx.doi.org/10.1128/jvi.00024-16.
Full textAbstract:
ABSTRACTThe potyviral RNA genome encodes two polyproteins that are proteolytically processed by three viral protease domains into 11 mature proteins. Extensive molecular studies have identified functions for the majority of the viral proteins. For example, 6K2, one of the two smallest potyviral proteins, is an integral membrane protein and induces the endoplasmic reticulum (ER)-originated replication vesicles that target the chloroplast for robust viral replication. However, the functional role of 6K1, the other smallest protein, remains uncharacterized. In this study, we developed a series of recombinant full-length viral cDNA clones derived from a CanadianPlum pox virus(PPV) isolate. We found that deletion of any of the short motifs of 6K1 (each of which ranged from 5 to 13 amino acids), most of the 6K1 sequence (but with the conserved sequence of the cleavage sites being retained), or all of the 6K1 sequence in the PPV infectious clone abolished viral replication. Thetransexpression of 6K1 or thecisexpression of a dislocated 6K1 failed to rescue the loss-of-replication phenotype, suggesting the temporal and spatial requirement of 6K1 for viral replication. Disruption of the N- or C-terminal cleavage site of 6K1, which prevented the release of 6K1 from the polyprotein, either partially or completely inhibited viral replication, suggesting the functional importance of the mature 6K1. We further found that green fluorescent protein-tagged 6K1 formed punctate inclusions at the viral early infection stage and colocalized with chloroplast-bound viral replicase elements 6K2 and NIb. Taken together, our results suggest that 6K1 is required for viral replication and is an important viral element of the viral replication complex at the early infection stage.IMPORTANCEPotyviruses account for more than 30% of known plant viruses and consist of many agriculturally important viruses. The genomes of potyviruses encode two polyproteins that are proteolytically processed into 11 mature proteins, with the majority of them having been at least partially functionally characterized. However, the functional role of a small protein named 6K1 remains obscure. In this study, we showed that deletion of 6K1 or a short motif/region of 6K1 in the full-length cDNA clones of plum pox virus abolishes viral replication and that mutation of the N- or C-terminal cleavage sites of 6K1 to prevent its release from the polyprotein greatly attenuates or completely inhibits viral replication, suggesting its important role in potyviral infection. We report that 6K1 forms punctate structures and targets the replication vesicles in PPV-infected plant leaf cells at the early infection stage. Our data reveal that 6K1 is an important viral protein of the potyviral replication complex.
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Bera, Sayanta, Gabriella D. Arena, Swayamjit Ray, Sydney Flannigan, and Clare L. Casteel. "The Potyviral Protein 6K1 Reduces Plant Proteases Activity during Turnip mosaic virus Infection." Viruses 14, no. 6 (June 20, 2022): 1341. http://dx.doi.org/10.3390/v14061341.
Full textAbstract:
Potyviral genomes encode just 11 major proteins and multifunctionality is associated with most of these proteins at different stages of the virus infection cycle. Some potyviral proteins modulate phytohormones and protein degradation pathways and have either pro- or anti-viral/insect vector functions. Our previous work demonstrated that the potyviral protein 6K1 has an antagonistic effect on vectors when expressed transiently in host plants, suggesting plant defenses are regulated. However, to our knowledge the mechanisms of how 6K1 alters plant defenses and how 6K1 functions are regulated are still limited. Here we show that the 6K1 from Turnip mosaic virus (TuMV) reduces the abundance of transcripts related to jasmonic acid biosynthesis and cysteine protease inhibitors when expressed in Nicotiana benthamiana relative to controls. 6K1 stability increased when cysteine protease activity was inhibited chemically, showing a mechanism to the rapid turnover of 6K1 when expressed in trans. Using RNAseq, qRT-PCR, and enzymatic assays, we demonstrate TuMV reprograms plant protein degradation pathways on the transcriptional level and increases 6K1 stability at later stages in the infection process. Moreover, we show 6K1 decreases plant protease activity in infected plants and increases TuMV accumulation in systemic leaves compared to controls. These results suggest 6K1 has a pro-viral function in addition to the anti-insect vector function we observed previously. Although the host targets of 6K1 and the impacts of 6K1-induced changes in protease activity on insect vectors are still unknown, this study enhances our understanding of the complex interactions occurring between plants, potyviruses, and vectors.
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Kang, Hara, Yong Jae Lee, Jae Hwan Goo, and Woo Jin Park. "Determination of the substrate specificity of turnip mosaic virus NIa protease using a genetic method." Journal of General Virology 82, no. 12 (December 1, 2001): 3115–17. http://dx.doi.org/10.1099/0022-1317-82-12-3115.
Full textAbstract:
The RNA genome of turnip mosaic potyvirus (TuMV) encodes a large polyprotein that is processed to mature proteins by virus-encoded proteases. The TuMV NIa protease is responsible for the cleavage of the polyprotein at seven different locations. These cleavage sites are defined by a conserved sequence motif Val-Xaa-His-Gln↓, with the scissile bond located after Gln. To determine the substrate specificity of the NIa protease, amino acid sequences cleaved by the NIa protease were obtained from randomized sequence libraries using a screening method referred to as GASP (genetic assay for site-specific proteolysis). Based on statistical analysis of the obtained sequences, a consensus substrate sequence was deduced: Yaa-Val-Arg-His-Gln↓Ser, with Yaa being an aliphatic amino acid and the scissile bond being located between Gln and Ser. This result is consistent with the conserved cleavage sequence motif, and should provide insight into the molecular activity of the NIa protease.
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Martín, María Teresa, Carlos López Otín, Sonia Laín, and Juan Antonio García. "Determination of polyprotein processing sites by amino terminal sequencing of nonstructural proteins encoded by plum pox potyvirus." Virus Research 15, no. 2 (February 1990): 97–106. http://dx.doi.org/10.1016/0168-1702(90)90001-r.
Full textDissertations / Theses on the topic "Potyviral Encoded Proteins"
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Sabharwal, Pallavi. "Molecular Insights into the Structure and Function of Pepper Vein Banding Virus Encoded Proteins and Endocytic Uptake Pathway of Virus-like Particles into Mammalian Cells." Thesis, 2017. http://etd.iisc.ac.in/handle/2005/4282.
Full textAbstract:
Viruses are major pathogenic agents that cause a variety of diseases in all living systems. Since their first isolation in 1892 by Dimitrii Ivanovsky, methods of their diagnosis and control, their life cycles, host - virus interactions, mechanisms of resistance etc have been intensely researched. The first virus ever to be discovered was Tobacco mosaic virus (TMV), a plant virus (Beijerinck, 1898). More than three thousand viruses that infect not only plants, but also humans, animals and bacteria have been described (Koonin et al., 2006 ; Lawrence et al., 2009; King et al., 2012). Over the years, study of viruses has shown that they are obligate parasites and their life cycle stages are analogous to the cellular processes. Interestingly, many of the concepts and tools of molecular biology have been derived from the study of viruses because of their small genomes. The structural and functional simplicity of viruses have made them attractive tools for scientists to study a variety of biological phenomena.
According to the ninth report of the International Committee on Taxonomy of Viruses (ICTV IX) (King et al., 2012) the number of recognized viruses is 3,618, of which ~25% (957) are plant viruses and they have been classified into different families (Fig.1.1). RNA viruses infecting plants are highly abundant and more diverse when compared to DNA viruses (Koonin et al., 2015). Single-stranded RNA viruses have been shown to generally have smaller genomes (average length ~9kb). While this allows the viruses to mutate and evolve faster (Sanjuán and Domingo-Calap, 2016), it also makes it essential for these viruses to encode for multifunctional proteins.
There are seven defined families of positive sense, single stranded RNA plant viruses, namely, Bromoviridae, Closteroviridae, Luteoviridae, Potyviridae, Seconaviridae, Tombusviridae, and Virgaviridae. Among these families, the family Potyviridae contains the largest group of plant viruses that are also economically very important (Martínez et al., 2016). Their genome organization and expression strategies are similar to picornaviruses (Domier et al., 1987) and are therefore classified along with picorna-like superfamily of viruses. According to ICTV classification, the family Potyviridae consists of eight genera and two unassigned species (Table 1.1) based on physical properties of virion, RNA sequence, genome organization and mode of transmission (Wylie et al., 2017). The genus Potyvirus named after its type species, Potato virus Y (Ward and Shukla, 1991; Riechmann et al., 1992) is one of the oldest and the most successful of all known genera comprising of 146 virus species.