Potyvirus proteins: a wealth of functions

Urcuqui-Inchima, Silvio; Haenni, Anne‐Lise; Bernardi, Françoise

doi:10.1016/s0168-1702(01)00220-9

Cited by 460 publications

(332 citation statements)

References 121 publications

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“…Potato virus A (PVA) belongs to Potyviridae (genus Potyvirus), the largest virus family infecting plants (Shukla et al 1994;Urcuqui-Inchima et al 2001). The PVA genome is composed of a messenger-polarity ssRNA of 9565 to 9572 nt including a 3Ј-poly(A) tail and a virus-encoded protein (VPg) covalently attached to the 5Ј-end (Kekarainen et al 1999;Oruetxebarria et al 2001).…”

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confidence: 99%

Functional Genomics on Potato Virus A: Virus Genome-Wide Map of Sites Essential for Virus Propagation

Kekarainen¹,

Savilahti²,

Valkonen³

2002

Genome Res.

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Transposition-based in vitro insertional mutagenesis strategies provide promising new approaches for functional characterization of any cloned gene or genome region. We have extended the methodology and scope of such analysis to a complete viral genome. To map genome regions both essential and nonessential for Potato virus A propagation, we generated a genomic 15-bp insertion mutant library utilizing the efficient in vitro DNA transposition reaction of phage Mu. We then determined the proficiency of 1125 mutants to propagate in tobacco protoplasts by using a genetic footprinting strategy that simultaneously mapped the genomic insertion sites. Over 300 sites critical for virus propagation were identified, and many of them were located in positions previously not assigned to any viral functions. Many genome regions tolerated insertions indicating less important sites for virus propagation and thus pinpointed potential locations for further genome manipulation. The methodology described is applicable to a detailed functional analysis of any viral nucleic acid cloned as DNA and can be used to address many different processes during viral infection cycles

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confidence: 99%

Functional Genomics on Potato Virus A: Virus Genome-Wide Map of Sites Essential for Virus Propagation

Kekarainen¹,

Savilahti²,

Valkonen³

2002

Genome Res.

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“…Potyvirus is the largest genus of plant viruses (reviewed by López-Moya et al, 2000;Urcuqui-Inchima et al, 2001) with several species, such as Potato virus Y (PVY), Plum pox virus (PPV) or Tobacco vein mottling virus (TVMV), causing severe agronomic losses. A series of VRTPs have been generated to control different potyviruses including the above-mentioned PVY (Lawson et al, 1990), TVMV (Moreno et al, 1998) and PPV (López-Moya et al, 2000), respectively.…”

Section: Dietrich Et Almentioning

confidence: 99%

No recombination detected in artificial potyvirus mixed infections and between potyvirus derived transgenes and heterologous challenging potyviruses

Dietrich

Miller²,

McKenzie³

et al. 2007

Environ. Biosafety Res.

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“…Potyviruses are positive-sense singlestranded RNA viruses and form the largest genus of plant virus (2). The genome of potyvirus is translated into a single large 340 -370-kDa polyprotein that contains in the N to C order 10 proteins: P1, HC-Pro, P3, 6K1, CI, 6K2, VPg, NIa-Pro, Nlb, and coat protein.…”

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confidence: 99%

“…The genome of potyvirus is translated into a single large 340 -370-kDa polyprotein that contains in the N to C order 10 proteins: P1, HC-Pro, P3, 6K1, CI, 6K2, VPg, NIa-Pro, Nlb, and coat protein. The polyprotein is processed into mature products by three virus-encoded proteases P1 (3,4), helper-component proteinase (HC-Pro) 2 (5,6), and NIa-Pro (7). P1 and HCPro cleave only at their respective C termini in cis, whereas NIa-Pro is a trypsin-like cysteine proteinase responsible for the remaining of seven cleavage events in the C-terminal twothirds of the polyprotein.…”

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confidence: 99%

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Structure of the Autocatalytic Cysteine Protease Domain of Potyvirus Helper-component Proteinase

Guo

Lin

2011

Journal of Biological Chemistry

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The helper-component proteinase (HC-Pro) of potyvirus is involved in polyprotein processing, aphid transmission, and suppression of antiviral RNA silencing. There is no high resolution structure reported for any part of HC-Pro, hindering mechanistic understanding of its multiple functions. We have determined the crystal structure of the cysteine protease domain of HC-Pro from turnip mosaic virus at 2.0 Å resolution. As a protease, HC-Pro only cleaves a Gly-Gly dipeptide at its own C terminus. The structure represents a postcleavage state in which the cleaved C terminus remains tightly bound at the active site cleft to prevent trans activity. The structure adopts a compact ␣/␤-fold, which differs from papain-like cysteine proteases and shows weak similarity to nsP2 protease from Venezuelan equine encephalitis alphavirus. Nevertheless, the catalytic cysteine and histidine residues constitute an active site that is highly similar to these in papain-like and nsP2 proteases. HC-Pro recognizes a consensus sequence YXVGG around the cleavage site between the two glycine residues. The structure delineates the sequence specificity at sites P1-P4. Structural modeling and covariation analysis across the Potyviridae family suggest a tryptophan residue accounting for the glycine specificity at site P1 . Moreover, a surface of the protease domain is conserved in potyvirus but not in other genera of the Potyviridae family, likely due to extra functional constrain. The structure provides insight into the catalysis mechanism, cis-acting mode, cleavage site specificity, and other functions of the HC-Pro protease domain.

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Potyvirus proteins: a wealth of functions

Cited by 460 publications

References 121 publications

Functional Genomics on Potato Virus A: Virus Genome-Wide Map of Sites Essential for Virus Propagation

Functional Genomics on Potato Virus A: Virus Genome-Wide Map of Sites Essential for Virus Propagation

No recombination detected in artificial potyvirus mixed infections and between potyvirus derived transgenes and heterologous challenging potyviruses

Structure of the Autocatalytic Cysteine Protease Domain of Potyvirus Helper-component Proteinase

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