메뉴 건너뛰기




Volumn 71, Issue 10, 1997, Pages 7258-7265

The N-terminal region of the luteovirus readthrough domain determines virus binding to Buchnera GroEL and is essential for virus persistence in the aphid

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN; VIRUS PROTEIN;

EID: 1842372081     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.10.7258-7265.1997     Document Type: Article
Times cited : (134)

References (71)
  • 2
    • 0025187346 scopus 로고
    • Expression of the genome of potato leafroll virus: Readthrough of the coat protein termination codon in vivo
    • Bahner, I., J. Lamb, M. A. Mayo, and R. T. Hay. 1990. Expression of the genome of potato leafroll virus: readthrough of the coat protein termination codon in vivo. J. Gen. Virol. 71:2251-2256.
    • (1990) J. Gen. Virol. , vol.71 , pp. 2251-2256
    • Bahner, I.1    Lamb, J.2    Mayo, M.A.3    Hay, R.T.4
  • 3
    • 0023761756 scopus 로고
    • Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein
    • Bochkareva, E. S., N. M. Lissin, and A. S. Girshovich. 1988. Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein. Nature 336:254-257.
    • (1988) Nature , vol.336 , pp. 254-257
    • Bochkareva, E.S.1    Lissin, N.M.2    Girshovich, A.S.3
  • 4
  • 7
    • 0343247747 scopus 로고    scopus 로고
    • Effects of mutations in the beet western yellows virus rcadthrough protein on its expression and packaging, and on virus accumulation, symptoms, and aphid transmission
    • Bruyère, A., V. Brault, V. Ziegler-Graff, M.-T. Simon is, J. F. J. M. van den Heuvel, K. Richards, H. Guilley, G. Jonard, and E. Herrbach. 1997. Effects of mutations in the beet western yellows virus rcadthrough protein on its expression and packaging, and on virus accumulation, symptoms, and aphid transmission. Virology 230:323-334.
    • (1997) Virology , vol.230 , pp. 323-334
    • Bruyère, A.1    Brault, V.2    Ziegler-Graff, V.3    Simon Is, M.-T.4    Van den Heuvel, J.F.J.M.5    Richards, K.6    Guilley, H.7    Jonard, G.8    Herrbach, E.9
  • 9
    • 0029941744 scopus 로고    scopus 로고
    • Aphid transmission and systemic plant infection determinants of barley yellow dwarf luteovirus-PAV are contained in the coat protein readthrough domain and 17-kDa protein, respectively
    • Chay, C. A., U. B. Gunasinge, S. P. Dinesh-Kumar, W. A. Miller, and S. M. Gray. 1996. Aphid transmission and systemic plant infection determinants of barley yellow dwarf luteovirus-PAV are contained in the coat protein readthrough domain and 17-kDa protein, respectively. Virology 219:57-65.
    • (1996) Virology , vol.219 , pp. 57-65
    • Chay, C.A.1    Gunasinge, U.B.2    Dinesh-Kumar, S.P.3    Miller, W.A.4    Gray, S.M.5
  • 10
    • 0028027055 scopus 로고
    • Localisation of a folding protein and shape charges in GroEL-GroES complexes imaged by cryoelectron microscopy
    • Chen, S., A. M. Roseman, A. S. Hunter, S. P. Wood, S. G. Burston, N. A. Ranson, A. R. Clarke, and H. R. Saibil. 1994. Localisation of a folding protein and shape charges in GroEL-GroES complexes imaged by cryoelectron microscopy. Nature 371:261-264.
    • (1994) Nature , vol.371 , pp. 261-264
    • Chen, S.1    Roseman, A.M.2    Hunter, A.S.3    Wood, S.P.4    Burston, S.G.5    Ranson, N.A.6    Clarke, A.R.7    Saibil, H.R.8
  • 11
    • 0023422894 scopus 로고
    • Host immunoglobulin G titre and antibody activity in haemolymph of the tick, Omithodoros moubata
    • Chinzei, Y., and H. Minoura. 1987. Host immunoglobulin G titre and antibody activity in haemolymph of the tick, Omithodoros moubata. Med. Vet. Entomol. 1:409-416.
    • (1987) Med. Vet. Entomol. , vol.1 , pp. 409-416
    • Chinzei, Y.1    Minoura, H.2
  • 12
    • 0031043444 scopus 로고    scopus 로고
    • Expression and suppression of circulative aphid transmission in pea enation mosaic virus
    • Demler, S. A., D. G. Rucker-Feeney, J. S. Skaf, and G. A. de Zoeten. 1997. Expression and suppression of circulative aphid transmission in pea enation mosaic virus. J. Gen. Virol. 72:511-523.
    • (1997) J. Gen. Virol. , vol.72 , pp. 511-523
    • Demler, S.A.1    Rucker-Feeney, D.G.2    Skaf, J.S.3    De Zoeten, G.A.4
  • 14
    • 0026545587 scopus 로고
    • Precise mapping and in vitro translation of a trifunctional subgenomic RNA of barley yellow dwarf virus
    • Dinesh-Kumar, S. P., V. Brault, and W. A. Miller. 1992. Precise mapping and in vitro translation of a trifunctional subgenomic RNA of barley yellow dwarf virus. Virology 187:711-722.
    • (1992) Virology , vol.187 , pp. 711-722
    • Dinesh-Kumar, S.P.1    Brault, V.2    Miller, W.A.3
  • 15
    • 1842368350 scopus 로고    scopus 로고
    • Personal communication
    • Douglas, A. E. Personal communication.
    • Douglas, A.E.1
  • 18
    • 0011676334 scopus 로고
    • Evidence for lack of propagation of potato leaf roll virus in its aphid vector, Myzus persicae
    • Eskandari, F., E. S. Sylvester, and J. Richardson. 1979. Evidence for lack of propagation of potato leaf roll virus in its aphid vector, Myzus persicae. Phytopathology 69:45-47.
    • (1979) Phytopathology , vol.69 , pp. 45-47
    • Eskandari, F.1    Sylvester, E.S.2    Richardson, J.3
  • 19
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton, W. A., Y. Kashi, K. Furtak, and A. L. Horwich. 1994. Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371:614-619.
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 20
    • 0031060556 scopus 로고    scopus 로고
    • In vitro interactions of the aphid endosymbiotic SymL chaperonin with barley yellow dwarf virus
    • Filichkin, S. A., S. Brumfield, T. P. Filichkin, and M. J. Young. 1997. In vitro interactions of the aphid endosymbiotic SymL chaperonin with barley yellow dwarf virus. J. Virol. 71:569-577.
    • (1997) J. Virol. , vol.71 , pp. 569-577
    • Filichkin, S.A.1    Brumfield, S.2    Filichkin, T.P.3    Young, M.J.4
  • 21
    • 0028135705 scopus 로고
    • In vivo expression and mutational analysis of the barley yellow dwarf virus readthrough gene
    • Filichkin, S. A., R. M. Lister, P. F. McGrath, and M. J. Young. 1994. In vivo expression and mutational analysis of the barley yellow dwarf virus readthrough gene. Virology 205:290-299.
    • (1994) Virology , vol.205 , pp. 290-299
    • Filichkin, S.A.1    Lister, R.M.2    McGrath, P.F.3    Young, M.J.4
  • 22
    • 0002084539 scopus 로고
    • Virus-membrane interactions involved in circulative transmission of luteoviruses by aphids, Curr
    • Gildow, F. E. 1987. Virus-membrane interactions involved in circulative transmission of luteoviruses by aphids, Curr. Top. Vector Res. 4:93-120.
    • (1987) Top. Vector Res. , vol.4 , pp. 93-120
    • Gildow, F.E.1
  • 23
    • 0027130636 scopus 로고
    • The aphid salivary gland basal lamina as a selective barrier associated with vector-specific transmission of barley yellow dwarf luteoviruses
    • Gildow, F. E., and S. M. Gray. 1993. The aphid salivary gland basal lamina as a selective barrier associated with vector-specific transmission of barley yellow dwarf luteoviruses. Phytopathology 83:1293-1302.
    • (1993) Phytopathology , vol.83 , pp. 1293-1302
    • Gildow, F.E.1    Gray, S.M.2
  • 24
    • 0024820705 scopus 로고
    • Reconstitution of active dimeric ribulose biphosphate carboxylasc from an unfolded state depends on two chaperonin proteins and Mg-ATP
    • Goloubinoff, P., J. T. Christeller, A. A. Gatenby, and G. H. Lorimer. 1989. Reconstitution of active dimeric ribulose biphosphate carboxylasc from an unfolded state depends on two chaperonin proteins and Mg-ATP. Nature 342:884-889.
    • (1989) Nature , vol.342 , pp. 884-889
    • Goloubinoff, P.1    Christeller, J.T.2    Gatenby, A.A.3    Lorimer, G.H.4
  • 25
    • 0028888268 scopus 로고
    • Nueleotide sequence of beet mild yellowing virus RNA
    • Guilley, H., K. E. Richards, and G. Jonard. 1995. Nueleotide sequence of beet mild yellowing virus RNA. Arch. Virol. 140:1109-1118.
    • (1995) Arch. Virol. , vol.140 , pp. 1109-1118
    • Guilley, H.1    Richards, K.E.2    Jonard, G.3
  • 26
    • 0027990401 scopus 로고
    • Nueleotide sequence of cucurbit aphid-borne yellows luteovims
    • Guilley, H., C. Wipf-Scheibel, K. Richards, H. Lecoq, and G. Jonard. 1994. Nueleotide sequence of cucurbit aphid-borne yellows luteovims. Virology 202:1012-1017.
    • (1994) Virology , vol.202 , pp. 1012-1017
    • Guilley, H.1    Wipf-Scheibel, C.2    Richards, K.3    Lecoq, H.4    Jonard, G.5
  • 27
    • 0000214606 scopus 로고
    • The predominant protein in an aphid cndosymbiont is homologous to an E. Coli Heat Shock Protein
    • Hara, E., T. Fukatsu, K. Kakeda, M. Kengaku, C. Ohtaka, and H. Ishikawa. 1990. The predominant protein in an aphid cndosymbiont is homologous to an E. coli heat shock protein. Symbiosis 8:271-283.
    • (1990) Symbiosis , vol.8 , pp. 271-283
    • Hara, E.1    Fukatsu, T.2    Kakeda, K.3    Kengaku, M.4    Ohtaka, C.5    Ishikawa, H.6
  • 28
    • 1842297414 scopus 로고
    • Purification and partial characterization of symbionin. an aphid endosymbiont-specific protein
    • Hara, E., and H. Ishikawa. 1990. Purification and partial characterization of symbionin. an aphid endosymbiont-specific protein. Insect Biochem. 20:421-427.
    • (1990) Insect Biochem. , vol.20 , pp. 421-427
    • Hara, E.1    Ishikawa, H.2
  • 29
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. 1996. Molecular chaperones in cellular protein folding. Nature 381:571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 30
    • 0028334547 scopus 로고
    • Conformational specificity of the chaperonin GroEL for the compact folding intermediates of a-lactalbumin
    • Hayer-Hartl, M. K., J. J. Ewbank, T. E. Creighton, and F. U. Haitl. 1994. Conformational specificity of the chaperonin GroEL for the compact folding intermediates of a-lactalbumin. EMBO J. 13:3192-3202.
    • (1994) EMBO J. , vol.13 , pp. 3192-3202
    • Hayer-Hartl, M.K.1    Ewbank, J.J.2    Creighton, T.E.3    Haitl, F.U.4
  • 31
    • 1842338533 scopus 로고    scopus 로고
    • Personal communication
    • 3L Herrbach, E. Personal communication.
    • Herrbach, E.1
  • 32
    • 0001202521 scopus 로고
    • Characterization of the protein species synthesized in vjvol and in vitro by an aphid endosymbiont
    • Ishikawa, H. 1984. Characterization of the protein species synthesized in vjvol and in vitro by an aphid endosymbiont. Insect Biochem. 14:417-425.
    • (1984) Insect Biochem. , vol.14 , pp. 417-425
    • Ishikawa, H.1
  • 33
    • 0028308047 scopus 로고
    • Changes in the amino acid sequence of the coat protein readthrough domain of potato leafroll luteovirus affect the formation of an epitope and aphid transmission
    • Jolly, C. A., and M. A. Mayo. 1994. Changes in the amino acid sequence of the coat protein readthrough domain of potato leafroll luteovirus affect the formation of an epitope and aphid transmission. Virology 201:182-185.
    • (1994) Virology , vol.201 , pp. 182-185
    • Jolly, C.A.1    Mayo, M.A.2
  • 34
    • 0025953952 scopus 로고
    • Molecular chaperon produced by an intracellular symbiont
    • Kakeda, K., and H. Ishikawa. 1991. Molecular chaperon produced by an intracellular symbiont. J. Biochem. 110:583-587.
    • (1991) J. Biochem. , vol.110 , pp. 583-587
    • Kakeda, K.1    Ishikawa, H.2
  • 35
    • 0027728318 scopus 로고
    • A simple and rapid method for the purification of GroEL, an Eschcrichia coli homolog of the heat shock protein 60 family of molecular chaperonins
    • Khandekar, S. S., B. M. Bettencourt, K. C. Kelley, and M. A. Recny. 1993. A simple and rapid method for the purification of GroEL, an Eschcrichia coli homolog of the heat shock protein 60 family of molecular chaperonins. Prot Expr. Purif. 4:580-584.
    • (1993) Prot Expr. Purif. , vol.4 , pp. 580-584
    • Khandekar, S.S.1    Bettencourt, B.M.2    Kelley, K.C.3    Recny, M.A.4
  • 36
    • 0026595140 scopus 로고
    • Different conformations for the same polypeptidc bound to the chaperons DnaK and GroEL
    • Landry, S. J., R. Jordan, R. MeMacken, and L. M. Gierasch, 1992. Different conformations for the same polypeptidc bound to the chaperons DnaK and GroEL Nature 355:455-457.
    • (1992) Nature , vol.355 , pp. 455-457
    • Landry, S.J.1    Jordan, R.2    Memacken, R.3    Gierasch, L.M.4
  • 37
    • 0027092285 scopus 로고
    • Chaperonin-mediated protein folding: GroES hinds to one end of the GroEL cylinder, which accommodates the protein substrate within it central cavity
    • Langer, T., G. Pfeifer, J. Martin, W. Baumeister, and FMJ. Hartl. 1991 Chaperonin-mediated protein folding: GroES hinds to one end of the GroEL cylinder, which accommodates the protein substrate within it central cavity. EMBO J. 11:4757-4765.
    • (1991) EMBO J. , vol.11 , pp. 4757-4765
    • Langer, T.1    Pfeifer, G.2    Martin, J.3    Baumeister, W.4    Hartl, F.5
  • 38
    • 0024449598 scopus 로고
    • Three pure chaperone proteins of Escherichia coli-SecB, trigger factor and GroEL-form soluble complexes with precursor proteins in vitro
    • Lecker, S., R. Lill, T. Ziegelhoffer, C. Georgopoulos, P. J. Bassford, Jr., C. A. Kumamota, and W. Wickner. 1989. Three pure chaperone proteins of Escherichia coli-SecB, trigger factor and GroEL-form soluble complexes with precursor proteins in vitro. HMBO J. 8:2703-2709.
    • (1989) HMBO J. , vol.8 , pp. 2703-2709
    • Lecker, S.1    Lill, R.2    Ziegelhoffer, T.3    Georgopoulos, C.4    Bassford Jr., P.J.5    Kumamota, C.A.6    Wickner, W.7
  • 40
    • 0028838951 scopus 로고
    • The Hydrophobie nature of GroEL-substrate binding
    • Lin, Z., F. P. Sehwartz, and E. Eisenstein. 1995. The Hydrophobie nature of GroEL-substrate binding. J. Biol. Chcm. 242:1011-1014.
    • (1995) J. Biol. Chcm. , vol.242 , pp. 1011-1014
    • Lin, Z.1    Sehwartz, F.P.2    Eisenstein, E.3
  • 41
    • 0028933373 scopus 로고
    • In vitro dissociation and self-assembly of three chaperonin 60s: The role of ATP
    • Lissin, N. M. 1995. In vitro dissociation and self-assembly of three chaperonin 60s: the role of ATP. FEBS Lett. 361:55-60.
    • (1995) FEBS Lett. , vol.361 , pp. 55-60
    • Lissin, N.M.1
  • 42
    • 0000498918 scopus 로고
    • Evaluation of indirect enzyme-linked immunosorbent assay for the detection of plant viruses
    • Lommel, S. A., A. H. McCain, and T. J. Morris. 1982. Evaluation of indirect enzyme-linked immunosorbent assay for the detection of plant viruses. Phytopathology 72:1018-1022.
    • (1982) Phytopathology , vol.72 , pp. 1018-1022
    • Lommel, S.A.1    McCain, A.H.2    Morris, T.J.3
  • 43
    • 0028605296 scopus 로고
    • The stability of the molecular chapcronin cpn60 is affected by site-directed replacement of cysteine 518
    • Luo, G.-X., and P. M. Horowitz. 1994. The stability of the molecular chapcronin cpn60 is affected by site-directed replacement of cysteine 518. J. Biol. Chem. 269:32151-32154.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32151-32154
    • Luo, G.-X.1    Horowitz, P.M.2
  • 44
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of GroEL through a 'molten-globule'-like intermediate
    • Martin, J., T. Langer, R. Boteva, A. Schramel, A. L. Honvich, and F.-U. Hartl. 1991. Chaperonin-mediated protein folding at the surface of GroEL through a 'molten-globule'-like intermediate. Nature 352:36-42.
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Honvich, A.L.5    Hartl, F.-U.6
  • 46
    • 0001365497 scopus 로고
    • Properties of monoclonal antibodies to potato leafroll luteovirus and their use to distinguish virus isolates differing in aphid transmissibility
    • Massalski, P. R., and B. D. Harrison. 1987. Properties of monoclonal antibodies to potato leafroll luteovirus and their use to distinguish virus isolates differing in aphid transmissibility. J. Gen. Virol. 68:1813-1821,
    • (1987) J. Gen. Virol. , vol.68 , pp. 1813-1821
    • Massalski, P.R.1    Harrison, B.D.2
  • 48
    • 0030050442 scopus 로고    scopus 로고
    • Molecular biology of luteoviruses
    • Mayo, M. A., and V. Ziegler-Graff. 1996. Molecular biology of luteoviruses. Virus Res. 46:413-460.
    • (1996) Virus Res. , vol.46 , pp. 413-460
    • Mayo, M.A.1    Ziegler-Graff, V.2
  • 49
    • 1842371924 scopus 로고
    • Studies on the properties of potato leaf roll virus by the aphid-injection method
    • Murayama, D., and M. Kojima. 1965. Studies on the properties of potato leaf roll virus by the aphid-injection method. Ann. Phytopathol, Soc. Jpn. 30:209-215.
    • (1965) Ann. Phytopathol, Soc. Jpn. , vol.30 , pp. 209-215
    • Murayama, D.1    Kojima, M.2
  • 50
    • 0026596164 scopus 로고
    • Structures of chaperonins from an intracellular symbiont and their functional expression in Escherichia coli groE mutants
    • Ohtaka, C., H. Nakamura, and H. Ishikawa. 1992. Structures of chaperonins from an intracellular symbiont and their functional expression in Escherichia coli groE mutants. J. Bacteriol. 174:1869-1874.
    • (1992) J. Bacteriol. , vol.174 , pp. 1869-1874
    • Ohtaka, C.1    Nakamura, H.2    Ishikawa, H.3
  • 51
    • 0027231696 scopus 로고
    • Antiviral melanization reaction of Heliothis vireseens hcmolymph against DNA and RNA viruses in vitro
    • Ourth, D. D., and H. E. Renis. 1993. Antiviral melanization reaction of Heliothis vireseens hcmolymph against DNA and RNA viruses in vitro. Comp. Biochem. Physiol. 1053:719-723.
    • (1993) Comp. Biochem. Physiol. , vol.1053 , pp. 719-723
    • Ourth, D.D.1    Renis, H.E.2
  • 52
    • 0028335861 scopus 로고
    • Soybean dwarf luteovirus contains the third variant genome type in the luteovirus group
    • Rathjen, J. P., L. E. Karageorgos, N. Habili, P. M. Waterhouse, and R. H. Symons. 1994, Soybean dwarf luteovirus contains the third variant genome type in the luteovirus group. Virology 198:671-679.
    • (1994) Virology , vol.198 , pp. 671-679
    • Rathjen, J.P.1    Karageorgos, L.E.2    Habili, N.3    Waterhouse, P.M.4    Symons, R.H.5
  • 53
    • 0027255147 scopus 로고
    • Identification of beet western yellows luteovirus genes implicated in viral replication and particle morphogenesis
    • Reutenauer, A., V. Ziegler-Graff, H. Lot, D. Scheidecker, H. Guilley, K. Richards, and G. Jonard. 1993. Identification of beet western yellows luteovirus genes implicated in viral replication and particle morphogenesis. Virology 195:692-699.
    • (1993) Virology , vol.195 , pp. 692-699
    • Reutenauer, A.1    Ziegler-Graff, V.2    Lot, H.3    Scheidecker, D.4    Guilley, H.5    Richards, K.6    Jonard, G.7
  • 54
    • 0000088832 scopus 로고
    • Barley yellow dwarf virus: Phenotypic mixing and vector specificity
    • Rochow, W. F. 1970. Barley yellow dwarf virus: phenotypic mixing and vector specificity. Science 167:875-878.
    • (1970) Science , vol.167 , pp. 875-878
    • Rochow, W.F.1
  • 55
    • 0242421150 scopus 로고
    • Aphids can acquire strains of barley yellow dwarf luteovirus they do not transmit
    • Rochow, W. F., and E. Pang, 1961. Aphids can acquire strains of barley yellow dwarf luteovirus they do not transmit. Virology 15:382-384.
    • (1961) Virology , vol.15 , pp. 382-384
    • Rochow, W.F.1    Pang, E.2
  • 56
    • 0026801563 scopus 로고
    • Interaction of GroE with an all-βprotein
    • Schmidt, M., and J. Buchner. 1992. Interaction of GroE with an all-βprotein. J. Biol. Chem. 267:16829-16833.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16829-16833
    • Schmidt, M.1    Buchner, J.2
  • 57
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 58
    • 0026527741 scopus 로고
    • Nucleotide sequence analysis of the genomes of the MAV- PSI and P-PAV isolates of barley yellow dwarf virus
    • Ueng, R P., J. R. Vincent, E. E. Kawata, C.-H. Lei, R. M. Lister, and B. A. Larkins. 1992. Nucleotide sequence analysis of the genomes of the MAV- PSI and P-PAV isolates of barley yellow dwarf virus, J. Gen. Virol. 73:487-492.
    • (1992) J. Gen. Virol. , vol.73 , pp. 487-492
    • Ueng, R.P.1    Vincent, J.R.2    Kawata, E.E.3    Lei, C.-H.4    Lister, R.M.5    Larkins, B.A.6
  • 59
  • 60
    • 0028830022 scopus 로고
    • Localization of potato leafroll virus in leaves of secondarily-infected potato plants
    • Van den Heuvel, J. F. J. M., C. M. de Blank, D. Peters, and J. W. M. van Lent. 1995. Localization of potato leafroll virus in leaves of secondarily-infected potato plants. Eur. J. Plant Path. 101:567-571.
    • (1995) Eur. J. Plant Path. , vol.101 , pp. 567-571
    • Van den Heuvel, J.F.J.M.1    De Blank, C.M.2    Peters, D.3    Van Lent, J.W.M.4
  • 61
    • 0027989755 scopus 로고
    • Endosymbiotic bacteria associated with circulative transmission of potato leafroll virus by Myzus persicae
    • Van den Heuvel, J. F. J. M., M. Verbeek, and F. van der Wilk. 1994. Endosymbiotic bacteria associated with circulative transmission of potato leafroll virus by Myzus persicae. J. Gen. Virol. 75:2559-2565.
    • (1994) J. Gen. Virol. , vol.75 , pp. 2559-2565
    • Van den Heuvel, J.F.J.M.1    Verbeek, M.2    Van der Wilk, F.3
  • 63
    • 0024120386 scopus 로고
    • Passage of host immunoglobulin G from blood meal into hemolymph of selected mosquito species (Diptera: Culicidae)
    • Vaughan, J. A., and A. F. Azad. 1988. Passage of host immunoglobulin G from blood meal into hemolymph of selected mosquito species (Diptera: Culicidae). J. Med. Entomol. 25:472-474.
    • (1988) J. Med. Entomol. , vol.25 , pp. 472-474
    • Vaughan, J.A.1    Azad, A.F.2
  • 64
    • 0025017685 scopus 로고
    • Quantitation of antisporozoite immunoglobulins in the hemolymph of Anopheles Stephensi after bloodfecding
    • Vaughan, J. A., R. A. Wirtz, V. E. do Rosario, and A. F. Azad. 1990. Quantitation of antisporozoite immunoglobulins in the hemolymph of Anopheles Stephensi after bloodfecding. Am. J. Trop. Med. Hyg. 42:10-16.
    • (1990) Am. J. Trop. Med. Hyg. , vol.42 , pp. 10-16
    • Vaughan, J.A.1    Wirtz, R.A.2    Do Rosario, V.E.3    Azad, A.F.4
  • 65
    • 0026542281 scopus 로고
    • Synthesis of full-length transcripts of beet western yellows virus RNA: Messenger properties and biological activity in protoplasts
    • Veidt, I., S. E. Bouzoubaa, R.-M. Leiser, V. Ziegler-Graff, H. Guilley, K. Richards, and G. Jonard. 1992. Synthesis of full-length transcripts of beet western yellows virus RNA: messenger properties and biological activity in protoplasts. Virology 186:192-200.
    • (1992) Virology , vol.186 , pp. 192-200
    • Veidt, I.1    Bouzoubaa, S.E.2    Leiser, R.-M.3    Ziegler-Graff, V.4    Guilley, H.5    Richards, K.6    Jonard, G.7
  • 68
    • 0028985008 scopus 로고
    • Readthrough protein associated with virions of barley yellow dwarf luteovirus and its potential role in regulating the efficiency of aphid transmission
    • Wang, J. Y., C. Chay, F. E. Gildow, and S. M. Gray. 1995. Readthrough protein associated with virions of barley yellow dwarf luteovirus and its potential role in regulating the efficiency of aphid transmission. Virology 206:954-962.
    • (1995) Virology , vol.206 , pp. 954-962
    • Wang, J.Y.1    Chay, C.2    Gildow, F.E.3    Gray, S.M.4
  • 69
    • 0029069914 scopus 로고
    • A mutant at position 87 of the GroEL chaperonin is affected in protein binding and ATP hydrolysis
    • Weiss, C., and P. Goloubinoff. 1995. A mutant at position 87 of the GroEL chaperonin is affected in protein binding and ATP hydrolysis. J. Biol. Chem. 270:13956-13960.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13956-13960
    • Weiss, C.1    Goloubinoff, P.2
  • 70
    • 0003488652 scopus 로고
    • Allen and Unwin, London, United Kingdom
    • Wright, C. A. 1971. Flukes and snails. Allen and Unwin, London, United Kingdom.
    • (1971) Flukes and Snails
    • Wright, C.A.1
  • 71
    • 0029832958 scopus 로고    scopus 로고
    • The coat protein of beet western yellows virus is essential for systemic infection but the viral gene products P29 and P19 are dispensable for systemic infection and aphid transmission
    • Ziegler-Graff, V., V. Brault, J. D. Mutterer, M.-T. Simonis, E. Herrbach, H. Guilley, K. E. Richards, and G. Jonard. 1996. The coat protein of beet western yellows virus is essential for systemic infection but the viral gene products P29 and P19 are dispensable for systemic infection and aphid transmission. Mol. Plant-Microbe Interact. 9:501-510.
    • (1996) Mol. Plant-Microbe Interact. , vol.9 , pp. 501-510
    • Ziegler-Graff, V.1    Brault, V.2    Mutterer, J.D.3    Simonis, M.-T.4    Herrbach, E.5    Guilley, H.6    Richards, K.E.7    Jonard, G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.