Interaction of a potyviral VPg with anionic phospholipid vesicles

Virology

Volumn 395, Issue 1, 2009, Pages 114-120

  Rantalainen, Kimmo I ^a   Christensen, Peter A ^b   Hafrén, Anders ^a   Otzen, Daniel E ^b   Kalkkinen, Nisse ^c   Mäkinen, Kristiina ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

^b The Interdisciplinary Nanoscience Centre   (Denmark)

^c UNIVERSITY OF HELSINKI   (Finland)

Author keywords

Anionic vesicles; Intrinsically disordered protein; Membrane interaction; Potato virus A; Potyvirus; VPg

Indexed keywords

MEMBRANE LIPID; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLSERINE; TRYPSIN; UNCLASSIFIED DRUG; VIRAL GENOME LINKED PROTEIN; VIRUS PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING ASSAY; CIRCULAR DICHROISM; ELECTRON MICROSCOPY; NONHUMAN; PHOSPHOLIPID VESICLE; POTATO VIRUS A; POTYVIRUS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN PROCESSING; PROTEIN SECONDARY STRUCTURE;

CIRCULAR DICHROISM; PHOSPHOLIPIDS; POTYVIRIDAE; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, SECONDARY; RIBONUCLEOPROTEINS; VIRAL NONSTRUCTURAL PROTEINS;

POTATO VIRUS A; POTYVIRUS;

EID: 71749093501     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2009.09.009     Document Type: Article

References (39)

1. Beauchemin C., Boutet N., and Laliberté J.F. Visualization of the interaction between the precursors of VPg, the viral protein linked to the genome of turnip mosaic virus, and the translation eukaryotic initiation factor iso 4E in planta. J. Virol. 81 (2007) 775-782
2. Bryson E.A., Rankin S.E., Carey M., Watts A., and Pinheiro T.J. Folding of apocytochrome c in lipid micelles: formation of alpha-helix precedes membrane insertion. Biochemistry 38 (1999) 9758-9767
3. Cotton S., Grangeon R., Thivierge K., Mathieu I., Ide C., Wei T., Wang A., and Laliberté J.F. Turnip mosaic virus RNA replication complex vesicles are mobile, align with microfilaments and are each derived from a single viral genome. J. Virol. 83 (2009) 10460-10471
4. Davidson W.S., Jonas A., Clayton D.F., and George J.M. Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 273 (1998) 9443-9449
5. Denison M.R. Seeking membranes: positive-strand RNA virus replication complexes. PLoS Biol. e270 (2008) 6
6. Dunker A.K., Lawson J.D., Brown C.J., Williams R.M., Romero P., Oh J.S., Oldfield C.J., Campen A.M., Ratliff C.M., Hipps K.W., Ausio J., Nissen M.S., Reeves R., Kang C., Kissinger C.R., Bailey R.W., Griswold M.D., Chiu W., Garner E.C., and Obradovic Z. Intrinsically disordered protein. J. Mol. Graph. Model. 19 (2001) 26-59
7. Dunoyer P., Thomas C., Harrison S., Revers F., and Maule A. A cysteine-rich plant protein potentiates potyvirus movement through an interaction with the virus genome-linked protein VPg. J. Virol. 78 (2004) 2301-2309
8. Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6 (2005) 197-208
9. Grzela R., Szolajska E., Ebel C., Madern D., Favier A., Wojtal I., Zagorski W., and Chroboczek J. Virulence factor of potato virus Y, genome-attached terminal protein VPg, is a highly disordered protein. J. Biol. Chem. 283 (2008) 213-221
10. Guo D., Rajamäki M.L., Saarma M., and Valkonen J.P. Towards a protein interaction map of potyviruses: protein interaction matrixes of two potyviruses based on the yeast two-hybrid system. J. Gen. Virol. 82 (2001) 935-939
11. Hafren A., and Mäkinen K. Purification of viral genome-linked protein VPg from potato virus A-infected plants reveals several post-translationally modified forms of the protein. J. Gen. Virol. 89 (2008) 1509-1518
12. Hebrard E., Bessin Y., Michon T., Longhi S., Uversky V.N., Delalande F., et al. Intrinsic disorder in viral proteins genome-linked: experimental and predictive analyses. Virol. J. 6 (2009) 23
13. Herce H.D., and Garcia A.E. Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 20805-20810
14. Hildebrand P.W., Lorenzen S., Goede A., and Preissner R. Analysis and prediction of helix-helix interactions in membrane channels and transporters. Proteins 64 (2006) 253-262
15. Ivanov K.I., Puustinen P., Merits A., Saarma M., and Mäkinen K. Phosphorylation down-regulates the RNA binding function of the coat protein of potato virus A. J. Biol. Chem. 276 (2001) 13530-13540
16. Kelly M.K., Jess T.J., and Price N.C. How to study proteins by circular dichroism. Biochim. Biophys. Acta 1751 (2005) 119-139
17. Kentsis A., and Sosnick T.R. Trifluoroethanol promotes helix formation by destabilizing backbone exposure: desolvation rather than native hydrogen bonding defines the kinetic pathway of dimeric coiled coil folding. Biochemistry 37 (1998) 14613-14622
18. Kjaer L., Giehm L., Heimburg T., and Otzen D. The influence of vesicle size and composition on alpha-synuclein structure and stability. Biophys. J. 96 (2009) 2857-2870
19. Kopek B.G., Perkins G., Miller D.J., Ellisman M.H., and Ahlquist P. Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle. PLoS Biol. e220 (2007) 5
20. Lama J., and Carrasco L. Screening for membrane-permeabilizing mutants of the poliovirus protein 3AB. J. Gen. Virol. 77 Pt 9 (1996) 2109-2119
21. Léonard S., Viel C., Beauchemin C., Daigneault N., Fortin M.G., and Laliberté J.F. Interaction of VPg-pro of turnip mosaic virus with the translation initiation factor 4E and the poly(A)-binding protein in planta. J. Gen. Virol. 85 (2004) 1055-1063
22. Merits A., Guo D., Jarvekulg L., and Saarma M. Biochemical and genetic evidence for interactions between potato A potyvirus-encoded proteins P1 and P3 and proteins of the putative replication complex. Virology 263 (1999) 15-22
23. Miller S., and Krijnse-Locker J. Modification of intracellular membrane structures for virus replication. Nat. Rev. Microbiol. 6 (2008) 363-374
24. Oruetxebarria I., Guo D., Merits A., Mäkinen K., Saarma M., and Valkonen J.P.T. Identification of the genome-linked protein in virions of Potato virus A, with comparison to other members in genus Potyvirus. Virus Res. 73 (2001) 130-132
25. Op De Beeck A., Montserret R., Duvet S., Cocquerel L., Cacan R., Barberot B., et al. The transmembrane domains of hepatitis C virus envelope glycoproteins E1 and E2 play a major role in heterodimerization. J. Biol. Chem. 275 (2000) 31428-31437
26. Paul A.V., van Boom J.H., Filippov D., and Wimmer E. Protein-primed RNA synthesis by purified poliovirus RNA polymerase. Nature 393 (1998) 280-284
27. Puustinen P., and Mäkinen K. Uridylylation of the potyvirus VPg by viral replicase NIb correlates with the nucleotide binding capacity of VPg. J. Biol. Chem. 279 (2004) 38103-38110
28. Puustinen P., Rajamäki M.L., Ivanov K.I., Valkonen J.P., and Mäkinen K. Detection of the potyviral genome-linked protein VPg in virions and its phosphorylation by host kinases. J. Virol. 76 (2002) 12703-12711
29. Rantalainen K.I., Uversky V.N., Permi P., Kalkkinen N., Dunker A.K., and Mäkinen K. Potato virus A genome-linked protein VPg is an intrinsically disordered molten globule-like protein with a hydrophobic core. Virology 377 (2008) 280-288
30. Roudet-Tavert G., Michon T., Walter J., Delaunay T., Redondo E., and Le Gall O. Central domain of a potyvirus VPg is involved in the interaction with the host translation initiation factor eIF4E and the viral protein HcPro. J. Gen. Virol. 88 (2007) 1029-1033
31. Russ W.P., and Engelman D.M. The GxxxG motif: a framework for transmembrane helix-helix association. J. Mol. Biol. 296 (2000) 911-919
32. Salonen A., Ahola T., and Kaariainen L. Viral RNA replication in association with cellular membranes. Curr. Top. Microbiol. Immunol. 285 (2005) 139-173
33. Satheshkumar P.S., Gayathri P., Prasad K., and Savithri H.S. "Natively unfolded" VPg is essential for sesbania mosaic virus serine protease activity. J. Biol. Chem. 280 (2005) 30291-30300
34. Schaad M.C., Jensen P.E., and Carrington J.C. Formation of plant RNA virus replication complexes on membranes: role of an endoplasmic reticulum-targeted viral protein. EMBO J. 16 (1997) 4049-4059
35. Senes A., Engel D.E., and DeGrado W.F. Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr. Opin. Struct. Biol. 14 (2004) 465-479
36. Suhy D.A., Giddings Jr. T.H., and Kirkegaard K. Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles. J. Virol. 74 (2000) 8953-8965
37. Thivierge K., Cotton S., Dufresne P.J., Mathieu I., Beauchemin C., Ide C., Fortin M.G., and Laliberté J.F. Eukaryotic elongation factor 1A interacts with turnip mosaic virus RNA-dependent RNA polymerase and VPg-pro in virus-induced vesicles. Virology 377 (2008) 216-225
38. Uversky V.N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci. 11 (2002) 739-756
39. Wittmann S., Chatel H., Fortin M.G., and Laliberté J.F. Interaction of the viral protein genome linked of turnip mosaic potyvirus with the translational eukaryotic initiation factor (iso) 4E of Arabidopsis thaliana using the yeast two-hybrid system. Virology 234 (1997) 84-92