P1 peptidase – a mysterious protein of family Potyviridae

Rohozková, Jana; Navrátil, Milan

doi:10.1007/s12038-011-9020-6

Cited by 36 publications

(26 citation statements)

References 110 publications

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“…P1 is the least conserved protein in PVV-phureja sharing 70-77% amino acid identity with homologs within the PVV group in agreement with previous observations, which showed P1 to be the protein most variable in size and sequence within the genus Potyvirus (Rohozková and Navrátil, 2011). A recent study in tobacco etch virus (TEV) has shown P1 to contain nucleolar localization and nuclear export signals that allow its traffi c in and out of the nucleus and nucleolus during infection (Martínez and Daròs, 2014).…”

Section: Genome Sequence Propertiessupporting

confidence: 87%

Genome sequence of a divergent Colombian isolate of potato virus V (PVV) infecting Solanum phureja

Gutiérrez¹,

Hj²,

M³

2016

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Summary. -Deep sequencing analysis of the transcriptome of a Solanum phureja cv. Criolla Colombia plant with symptoms typical of a virus disease revealed an infection with potato virus V (PVV). Th e PVV-phureja genome comprises 9904 nt, exhibits 83% nucleotide identity with currently fully sequenced PVV isolates and contains one large ORF that codes for a polyprotein of 3065 residues fl anked by 5' and 3' UTR of 217 and 448 nt, respectively. Phylogenetic analysis of the PVV-phureja polyprotein indicates that it is divergent with respect to most PVV isolates. Th is is the fi rst complete PVV genome of an isolate infecting a host diff erent to S. tuberosum and, to this date, the only one from the South American Andes.

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Section: Genome Sequence Propertiessupporting

confidence: 87%

Genome sequence of a divergent Colombian isolate of potato virus V (PVV) infecting Solanum phureja

Gutiérrez¹,

Hj²,

M³

2016

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“…Besides the self-cleavage activity intrinsic to its C-terminal end, other activities of potyviral P1 and its real contributions to viral replication remained vague, so much so that P1 earned the appellative “mysterious protein” in a recent review [24].…”

Section: Discussionmentioning

confidence: 99%

The Hypervariable Amino-Terminus of P1 Protease Modulates Potyviral Replication and Host Defense Responses

2014

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The replication of many RNA viruses involves the translation of polyproteins, whose processing by endopeptidases is a critical step for the release of functional subunits. P1 is the first protease encoded in plant potyvirus genomes; once activated by an as-yet-unknown host factor, it acts in cis on its own C-terminal end, hydrolyzing the P1-HCPro junction. Earlier research suggests that P1 cooperates with HCPro to inhibit host RNA silencing defenses. Using Plum pox virus as a model, we show that although P1 does not have a major direct role in RNA silencing suppression, it can indeed modulate HCPro function by its self-cleavage activity. To study P1 protease regulation, we used bioinformatic analysis and in vitro activity experiments to map the core C-terminal catalytic domain. We present evidence that the hypervariable region that precedes the protease domain is predicted as intrinsically disordered, and that it behaves as a negative regulator of P1 proteolytic activity in in vitro cleavage assays. In viral infections, removal of the P1 protease antagonistic regulator is associated with greater symptom severity, induction of salicylate-dependent pathogenesis-related proteins, and reduced viral loads. We suggest that fine modulation of a viral protease activity has evolved to keep viral amplification below host-detrimental levels, and thus to maintain higher long-term replicative capacity.

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“…NIb is the viral RNA-dependent RNA polymerase (14), and CP, in addition to virion assembly, is involved in aphid transmission (15) and viral movement (16). In contrast, P1, the first product of potyviral polyprotein, is a rather mysterious protein whose functions during the infectious cycle are mostly unknown (17). The P1 cistron is the most variable in size and sequence in the various species of the genus (18).…”

Section: In This Work We Researched the Role During Infection Of Tobmentioning

confidence: 99%

Tobacco etch virus Protein P1 Traffics to the Nucleolus and Associates with the Host 60S Ribosomal Subunits during Infection

Martínez

Daròs

2014

J Virol

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The genus Potyvirus comprises a large group of positive-strand RNA plant viruses whose genome encodes a large polyprotein processed by three viral proteinases. P1 protein, the most amino-terminal product of the polyprotein, is an accessory factor stimulating viral genome amplification whose role during infection is not well understood. We infected plants with Tobacco etch virus (TEV; genus Potyvirus) clones in which P1 was tagged with a fluorescent protein to track its expression and subcellular localization or with an affinity tag to identify host proteins involved in complexes in which P1 also takes part during infection. Our results showed that TEV P1 exclusively accumulates in infected cells at an early stage of infection and that the protein displays a dynamic subcellular localization, trafficking in and out of the nucleus and nucleolus during infection. Inside the nucleolus, P1 particularly targets the dense granular component. Consistently, we found functional nucleolar localization and nuclear export signals in TEV P1 sequence. Our results also indicated that TEV P1 physically interacts with the host 80S cytoplasmic ribosomes and specifically binds to the 60S ribosomal subunits during infection. In vitro translation assays of reporter proteins suggested that TEV P1 stimulates protein translation, particularly when driven from the TEV internal ribosome entry site. These in vitro assays also suggested that TEV helper-component proteinase (HC-Pro) inhibits protein translation. Based on these findings, we propose that TEV P1 stimulates translation of viral proteins in infected cells. IMPORTANCEIn this work, we researched the role during infection of tobacco etch virus P1 protease. P1 is the most mysterious protein of potyviruses, a relevant group of RNA viruses infecting plants. Our experiments showed that the viral P1 protein exclusively accumulates in infected cells at an early stage of infection and moves in and out of the nucleus of infected cells, particularly targeting the nucleolus. Our experiments also showed that P1 protein binds host ribosomes during infection. Based on these findings and other in vitro experiments we propose that P1 protein stimulates translation of viral proteins during infection.

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P1 peptidase – a mysterious protein of family Potyviridae

Cited by 36 publications

References 110 publications

Genome sequence of a divergent Colombian isolate of potato virus V (PVV) infecting Solanum phureja

Genome sequence of a divergent Colombian isolate of potato virus V (PVV) infecting Solanum phureja

The Hypervariable Amino-Terminus of P1 Protease Modulates Potyviral Replication and Host Defense Responses

Tobacco etch virus Protein P1 Traffics to the Nucleolus and Associates with the Host 60S Ribosomal Subunits during Infection

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