The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review


Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Potyvirus


High impact information on Potyvirus

  • All proteins encoded by the plant potyvirus, tobacco etch virus (TEV), arise by proteolytic processing of a single polyprotein [6].
  • The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants [7].
  • The tobacco etch potyvirus protein, helper component-proteinase (HC-Pro), suppresses PTGS of silenced transgenes [8].
  • Five of the 11 subfamilies have thus far been mapped to the vicinity of known soybean genes for resistance to potyviruses (Rsv1 and Rpv), Phytophthora root rot (Rps1, Rps2, and Rps3), and powdery mildew (rmd) [9].
  • Tagging of plant potyvirus replication and movement by insertion of beta-glucuronidase into the viral polyprotein [10].

Chemical compound and disease context of Potyvirus

  • Comparison of the sequences of other potyviruses suggests that the presence of a glycine residue at the third position of the Asp-Ala-Gly triplet is critical for aphid transmissibility and that certain changes in the residues adjacent to this position abolish or greatly reduce aphid transmissibility [11].
  • The potyvirus cylindrical inclusion (CI) protein, an RNA helicase required for genome replication, was analyzed genetically using alanine-scanning mutagenesis [12].
  • Isolation and stability of histidine-tagged proteins produced in plants via potyvirus gene vectors [13].
  • The cleavage site between the 6K protein and the 49K proteinase is proposed to occur at the C-terminal side of glutamic acid and not at the C-terminal side of glutamine as in other potyviruses [14].
  • The first approximately 60 amino acids of the N-terminal part of the potyvirus helper component-proteinase (HC-Pro) include highly conserved residues comprising a Cys-rich region [15].

Biological context of Potyvirus

  • Infectious RNA transcripts were generated from full-length cDNA clones of the tobacco etch potyvirus genome containing an insertion of the bacterial beta-glucuronidase (GUS) gene between the polyprotein-coding sequences for the N-terminal 35-kDa proteinase and the helper component-proteinase [10].
  • Our results suggest that, in addition to its importance in aphid transmission, the HC-Pro gene may be of general importance in regulating virulence of potyviruses, possibly by interaction of these sequences with the host [16].
  • The plum pox potyvirus (PPV) protein CI is an RNA helicase whose function in the viral life cycle is still unknown [17].
  • Using a reverse genetic approach, the genome-linked protein of LMV, a multifunctional protein shown to be involved in viral genome amplification and movement of potyviruses, was established as the viral determinant responsible for the ability to overcome the resistance of the Niederzenz accession to LMV-0 [18].
  • A mutant (P1-616) of the tobacco vein mottling potyvirus that contains a four-codon insertion in the P1 protein coding region of the viral RNA is unable to infect the normal host plant of the virus [19].

Anatomical context of Potyvirus

  • Nuclear inclusion protein a (Nla) protease of turnip mosaic potyvirus is responsible for the processing of the viral polyprotein into functional proteins [20].

Gene context of Potyvirus

  • The locus associated with decreased susceptibility was named loss-of-susceptibility to potyviruses 1 (lsp1) [21].
  • The primary structure of the polyprotein was compared with that of other viral polyproteins, revealing the same general genetic organization as that of other picorna-like viruses (comoviruses, potyviruses and picornaviruses), except that an additional protein is suspected to occupy the N-terminus of the polyprotein [22].
  • Together with previous data showing that the VPg-eIF4E interaction is necessary for virus infectivity and upregulates genome amplification, this shows that the eIF4E proteins are specifically recruited for the replication cycle of potyviruses [23].
  • Comparison of the PVY polyprotein sequence with that of other potyvirus polyproteins shows similarities in genome organization and a high level of identity along most of the polyprotein, except for the putative proteins flanking the helper component [24].
  • Putative proteolytic cleavage sites were identified in the polyprotein of PSbMV by comparison with those identified for other potyviruses [14].

Analytical, diagnostic and therapeutic context of Potyvirus


  1. Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications. Bazan, J.F., Fletterick, R.J. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  2. Structural characterization of HC-Pro, a plant virus multifunctional protein. Plisson, C., Drucker, M., Blanc, S., German-Retana, S., Le Gall, O., Thomas, D., Bron, P. J. Biol. Chem. (2003) [Pubmed]
  3. RNA helicase activity of the plum pox potyvirus CI protein expressed in Escherichia coli. Mapping of an RNA binding domain. Fernández, A., Laín, S., García, J.A. Nucleic Acids Res. (1995) [Pubmed]
  4. Plant viral suppressors of post-transcriptional silencing do not suppress transcriptional silencing. Marathe, R., Smith, T.H., Anandalakshmi, R., Bowman, L.H., Fagard, M., Mourrain, P., Vaucheret, H., Vance, V.B. Plant J. (2000) [Pubmed]
  5. The 3C-like proteinase of an invertebrate nidovirus links coronavirus and potyvirus homologs. Ziebuhr, J., Bayer, S., Cowley, J.A., Gorbalenya, A.E. J. Virol. (2003) [Pubmed]
  6. Expression of potyviral polyproteins in transgenic plants reveals three proteolytic activities required for complete processing. Carrington, J.C., Freed, D.D., Oh, C.S. EMBO J. (1990) [Pubmed]
  7. The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants. Gutierrez-Campos, R., Torres-Acosta, J.A., Saucedo-Arias, L.J., Gomez-Lim, M.A. Nat. Biotechnol. (1999) [Pubmed]
  8. Virus-encoded suppressor of posttranscriptional gene silencing targets a maintenance step in the silencing pathway. Llave, C., Kasschau, K.D., Carrington, J.C. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  9. Isolation of a superfamily of candidate disease-resistance genes in soybean based on a conserved nucleotide-binding site. Yu, Y.G., Buss, G.R., Maroof, M.A. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  10. Tagging of plant potyvirus replication and movement by insertion of beta-glucuronidase into the viral polyprotein. Dolja, V.V., McBride, H.J., Carrington, J.C. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  11. Amino acid substitutions in the coat protein result in loss of insect transmissibility of a plant virus. Atreya, P.L., Atreya, C.D., Pirone, T.P. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  12. Genetic evidence for an essential role for potyvirus CI protein in cell-to-cell movement. Carrington, J.C., Jensen, P.E., Schaad, M.C. Plant J. (1998) [Pubmed]
  13. Isolation and stability of histidine-tagged proteins produced in plants via potyvirus gene vectors. Dolja, V.V., Peremyslov, V.V., Keller, K.E., Martin, R.R., Hong, J. Virology (1998) [Pubmed]
  14. The complete nucleotide sequence of pea seed-borne mosaic virus RNA. Johansen, E., Rasmussen, O.F., Heide, M., Borkhardt, B. J. Gen. Virol. (1991) [Pubmed]
  15. Effect of mutations within the cys-rich region of potyvirus helper component-proteinase on self-interaction. Urcuqui-Inchima, S., Maia, I.G., Drugeon, G., Haenni, A.L., Bernardi, F. J. Gen. Virol. (1999) [Pubmed]
  16. Mutational analysis of the helper component-proteinase gene of a potyvirus: effects of amino acid substitutions, deletions, and gene replacement on virulence and aphid transmissibility. Atreya, C.D., Pirone, T.P. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  17. The motif V of plum pox potyvirus CI RNA helicase is involved in NTP hydrolysis and is essential for virus RNA replication. Fernández, A., Guo, H.S., Sáenz, P., Simón-Buela, L., Gómez de Cedrón, M., García, J.A. Nucleic Acids Res. (1997) [Pubmed]
  18. Multiple resistance phenotypes to Lettuce mosaic virus among Arabidopsis thaliana accessions. Revers, F., Guiraud, T., Houvenaghel, M.C., Mauduit, T., Le Gall, O., Candresse, T. Mol. Plant Microbe Interact. (2003) [Pubmed]
  19. Infectious virus in transgenic plants inoculated with a nonviable, P1-proteinase defective mutant of a potyvirus. Moreno, M., Brandwagt, B.F., Shaw, J.G., Rodríguez-Cerezo, E. Virology (1999) [Pubmed]
  20. Characterization of Nla protease from turnip mosaic potyvirus exhibiting a low-temperature optimum catalytic activity. Kim, D.H., Hwang, D.C., Kang, B.H., Lew, J., Choi, K.Y. Virology (1996) [Pubmed]
  21. Loss-of-susceptibility mutants of Arabidopsis thaliana reveal an essential role for eIF(iso)4E during potyvirus infection. Lellis, A.D., Kasschau, K.D., Whitham, S.A., Carrington, J.C. Curr. Biol. (2002) [Pubmed]
  22. Nucleotide sequence of Hungarian grapevine chrome mosaic nepovirus RNA1. Le Gall, O., Candresse, T., Brault, V., Dunez, J. Nucleic Acids Res. (1989) [Pubmed]
  23. The Arabidopsis eukaryotic initiation factor (iso)4E is dispensable for plant growth but required for susceptibility to potyviruses. Duprat, A., Caranta, C., Revers, F., Menand, B., Browning, K.S., Robaglia, C. Plant J. (2002) [Pubmed]
  24. Nucleotide sequence of potato virus Y (N Strain) genomic RNA. Robaglia, C., Durand-Tardif, M., Tronchet, M., Boudazin, G., Astier-Manifacier, S., Casse-Delbart, F. J. Gen. Virol. (1989) [Pubmed]
  25. Identification of essential residues in potyvirus proteinase HC-Pro by site-directed mutagenesis. Oh, C.S., Carrington, J.C. Virology (1989) [Pubmed]
  26. Switches in the mode of transmission select for or against a poorly aphid-transmissible strain of potato virus Y with reduced helper component and virus accumulation. Legavre, T., Maia, I.G., Casse-Delbart, F., Bernardi, F., Robaglia, C. J. Gen. Virol. (1996) [Pubmed]
  27. Monitoring fusion protein cleavage by capillary electrophoresis. Bryant, J.D., McGhie, T.K., Smith, G.R. BioTechniques (1993) [Pubmed]
WikiGenes - Universities