Potyviruses (Potyviridae)

Vallí, Adrián; Garcı́a, Juan Antonio; López‐Moya, Juan José

doi:10.1016/b978-0-12-809633-8.21252-1

Cited by 17 publications

(10 citation statements)

References 17 publications

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“…With more than 200 assigned members sorted in 12 different genera, these viruses represent a major threat for basically every important crop on earth. Potyvirids (members of the family Potyviridae ) share common features, such as (i) monopartite (except for a few bipartite viruses) and positive sense single-stranded RNA (+ssRNA) genome, (ii) transmission mediated by vectors, and (iii) picorna-like gene expression strategy based on large polyproteins further processed by viral-encoded proteinases (Revers and García, 2015, Yang et al, 2021, Valli et al, 2021). Potyvirids, in most cases, produce 10 mature proteins: P1, HCPro, P3, P3N-PIPO, 6K1, CI, 6K2, NIa (VPg/NIaPro), NIb and CP.…”

Section: Introductionmentioning

confidence: 99%

Maf/ham1-like pyrophosphatases of non-canonical nucleotides are host-specific partners of viral RNA-dependent RNA polymerases

Vallí

López

Ribaya

et al. 2021

Preprint

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Cassava brown streak disease (CBSD), dubbed the Ebola of plants, is a serious threat for food security in Africa caused by two viruses of the family Potyviridae: cassava brown streak virus (CBSV) and Ugandan (U)CBSV. Intriguingly, U/CBSV, along with another member of this family and one secoviridae, are the only known RNA viruses in nature encoding a protein of the Maf/ham1-like family, a group of widespread pyrophosphatase of non-canonical nucleotides (ITPase) expressed by all living organisms. Despite the socio-economic impact of CDSD, the relevance and role of this atypical viral factor has not been yet established. Here, using an infectious cDNA clone and reverse genetics, we demonstrate that UCBSV requires the ITPase activity in cassava, but not in the model plant Nicotiana benthamiana. HPLC-MS/MS experiments show that, quite likely, this host-specific constraint is due to an unexpected high concentration of non-canonical nucleotides in cassava. Finally, protein analyses and experimental evolution of mutant viruses indicate that keeping a fraction of the yielded UCBSV ITPase covalently bound to the viral RNA-dependent RNA polymerase (RdRP) optimizes viral fitness, and this seems to be a feature shared by the other members of the Potyviridae family expressing Maf/ham1-like proteins. All in all, our work (i) reveals that the over-accumulation of non-canonical nucleotides in the host might have a key role in antiviral defense, and (ii) provides the first example of an RdRP-ITPase partnership, reinforcing the idea that RNA viruses are incredibly inventive at adaptation to different host setups.

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Section: Introductionmentioning

confidence: 99%

Maf/ham1-like pyrophosphatases of non-canonical nucleotides are host-specific partners of viral RNA-dependent RNA polymerases

Vallí

López

Ribaya

et al. 2021

Preprint

View full text Add to dashboard Cite

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Section: Discussionmentioning

confidence: 99%

“…The family Potyviridae comprises 10 genera and over 210 plant-infecting virus species, which can infect the most economically important crops in the world [ 26 ]. Most viruses in this family have single-stranded monopartite positive-sense RNA genomes, except for bipartite bymoviruses [ 2 , 26 ]. To date, studies on P3N-PIPO frameshift expression have been limited in the genus Potyvirus , and it remains unknown whether a similar frameshift expression of P3N-PIPO occurs in other genera in Potyviridae .…”

Section: Discussionmentioning

confidence: 99%

Integrated Proteomics and Transcriptomics Analyses Reveal the Transcriptional Slippage of a Bymovirus P3N-PIPO Gene Expressed from a PVX Vector in Nicotiana benthamiana

Chen

Miao

et al. 2021

Viruses

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P3N-PIPO (P3 N-terminal fused with Pretty Interesting Potyviridae ORF), the movement protein of potyviruses, is expressed as a translational fusion with the N-terminus of P3 in potyviruses. As reported in previous studies, P3N-PIPO is expressed via transcriptional slippage at a conserved G2A6 slippery site in the genus Potyvirus. However, it is still unknown whether a similar expression mechanism of P3N-PIPO is used in the other genera of the family Potyviridae. Moreover, due to the extremely low expression level of P3N-PIPO in natural virus-infected plants, the peptides spanning the slippery site which provide direct evidence of the slippage at the protein level, have not been identified yet. In this study, a potato virus X (PVX)-based expression vector was utilized to investigate the expression mechanism of P3N-PIPO. A high expression level of the P3N-PIPO(WT) of turnip mosaic virus (TuMV, genus Potyvirus) was observed based on the PVX expression vector. For the first time, we successfully identified the peptides of P3N-PIPO spanning the slippery site by mass spectrometry. Likewise, the P3N-PIPO(WT) of wheat yellow mosaic virus (WYMV, genus Bymovirus) was also successfully expressed using the PVX expression vector. Integrated proteome and transcriptome analyses revealed that WYMV P3N-PIPO was expressed at the conserved G2A6 site through transcriptional slippage. Moreover, as revealed by mutagenesis analysis, Hexa-adenosine of the G2A6 site was important for the frameshift expression of P3N-PIPO in WYMV. According to our results, the PVX-based expression vector might be used as an excellent tool to study the expression mechanism of P3N-PIPO in Potyviridae. To the best of our knowledge, this is the first experimental evidence for the expression mechanism of P3N-PIPO in the genus Bymovirus, the only genus comprising bipartite virus species in the family Potyviridae.

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“…The genus Potyvirus (family Potyviridae), is one of the most important groups of plant viruses [13]. The genome of potyviruses is a positive-sense single-stranded RNA of~10 kb, whose 5 end remains attached to the viral genome-linked protein (VPg) [14].…”

Section: Of 19mentioning

confidence: 99%

Virus Host Jumping Can Be Boosted by Adaptation to a Bridge Plant Species

et al. 2021

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Understanding biological mechanisms that regulate emergence of viral diseases, in particular those events engaging cross-species pathogens spillover, is becoming increasingly important in virology. Species barrier jumping has been extensively studied in animal viruses, and the critical role of a suitable intermediate host in animal viruses-generated human pandemics is highly topical. However, studies on host jumping involving plant viruses have been focused on shifting intra-species, leaving aside the putative role of “bridge hosts” in facilitating interspecies crossing. Here, we take advantage of several VPg mutants, derived from a chimeric construct of the potyvirus Plum pox virus (PPV), analyzing its differential behaviour in three herbaceous species. Our results showed that two VPg mutations in a Nicotiana clevelandii-adapted virus, emerged during adaptation to the bridge-host Arabidopsis thaliana, drastically prompted partial adaptation to Chenopodium foetidum. Although both changes are expected to facilitate productive interactions with eIF(iso)4E, polymorphims detected in PPV VPg and the three eIF(iso)4E studied, extrapolated to a recent VPg:eIF4E structural model, suggested that two adaptation ways can be operating. Remarkably, we found that VPg mutations driving host-range expansion in two non-related species, not only are not associated with cost trade-off constraints in the original host, but also improve fitness on it.

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Potyviruses (Potyviridae)

Cited by 17 publications

References 17 publications

Maf/ham1-like pyrophosphatases of non-canonical nucleotides are host-specific partners of viral RNA-dependent RNA polymerases

Maf/ham1-like pyrophosphatases of non-canonical nucleotides are host-specific partners of viral RNA-dependent RNA polymerases

Integrated Proteomics and Transcriptomics Analyses Reveal the Transcriptional Slippage of a Bymovirus P3N-PIPO Gene Expressed from a PVX Vector in Nicotiana benthamiana

Virus Host Jumping Can Be Boosted by Adaptation to a Bridge Plant Species

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