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Volumn 85, Issue 20, 2011, Pages 10710-10718

In situ cleavage of baculovirus occlusion-derived virus receptor binding protein p74 in the peroral infectivity complex

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PROTEINASE; MEMBRANE PROTEIN; PROTEIN P74; TRYPSIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 80054978392     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05110-11     Document Type: Article
Times cited : (23)

References (44)
  • 2
    • 65249097210 scopus 로고    scopus 로고
    • Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites
    • Belouzard, S., V. C. Chu, and G. R. Whittaker. 2009. Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites. Proc. Natl. Acad. Sci. U. S. A. 106:5871-5876.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 5871-5876
    • Belouzard, S.1    Chu, V.C.2    Whittaker, G.R.3
  • 3
    • 60149088309 scopus 로고    scopus 로고
    • Polydnaviruses of braconid wasps derive from an ancestral nudivirus
    • Bezier, A., et al. 2009. Polydnaviruses of braconid wasps derive from an ancestral nudivirus. Science 323:926-930.
    • (2009) Science , vol.323 , pp. 926-930
    • Bezier, A.1
  • 4
    • 0018762274 scopus 로고
    • Subunit protein and alkaline protease of entomopoxvirus spheroids
    • Bilimoria, S. L., and B. M. Arif. 1979. Subunit protein and alkaline protease of entomopoxvirus spheroids. Virology 96:596-603.
    • (1979) Virology , vol.96 , pp. 596-603
    • Bilimoria, S.L.1    Arif, B.M.2
  • 5
    • 0029398504 scopus 로고
    • Production of polyhedra of the Autographa californica nuclear polyhedrosis virus using the Sf21 and Tn5B1-4 cell lines and comparison with host-derived polyhedra by bioassay
    • Bonning, B. C., K. Hoover, S. Duffey, and B. D. Hammock. 1995. Production of polyhedra of the Autographa californica nuclear polyhedrosis virus using the Sf21 and Tn5B1-4 cell lines and comparison with host-derived polyhedra by bioassay. J. Invertebr. Pathol. 66:224-230.
    • (1995) J. Invertebr. Pathol. , vol.66 , pp. 224-230
    • Bonning, B.C.1    Hoover, K.2    Duffey, S.3    Hammock, B.D.4
  • 6
    • 77951983109 scopus 로고    scopus 로고
    • Cleavage of influenza virus hemagglutinin by airway proteases TMPRSS2 and HAT differs in subcellular localization and susceptibility to protease inhibitors
    • Bottcher-Friebertshauser, E., et al. 2010. Cleavage of influenza virus hemagglutinin by airway proteases TMPRSS2 and HAT differs in subcellular localization and susceptibility to protease inhibitors. J. Virol. 84:5605-5614.
    • (2010) J. Virol. , vol.84 , pp. 5605-5614
    • Bottcher-Friebertshauser, E.1
  • 7
    • 0017703554 scopus 로고
    • Effect of alkaline protease on the antigenic nature of wiseana nuclear polyhedrosis virus polyhedron protein
    • Crawford, A. M., and J. Kalmakoff. 1977. Effect of alkaline protease on the antigenic nature of wiseana nuclear polyhedrosis virus polyhedron protein. J. Virol. 24:412-415.
    • (1977) J. Virol. , vol.24 , pp. 412-415
    • Crawford, A.M.1    Kalmakoff, J.2
  • 8
    • 0016716759 scopus 로고
    • Degradation of matrix protein from a nuclear-polyhedrosis virus of Trichoplusia ni by an endogenous protease
    • Eppstein, D. A., J. A. Thoma, H. A. Scott, and S. Y. Young III. 1975. Degradation of matrix protein from a nuclear-polyhedrosis virus of Trichoplusia ni by an endogenous protease. Virology 67:591-594.
    • (1975) Virology , vol.67 , pp. 591-594
    • Eppstein, D.A.1    Thoma, J.A.2    Scott, H.A.3    Young III, S.Y.4
  • 9
    • 70450195117 scopus 로고    scopus 로고
    • Autographa californica multiple nucleopolyhedrovirus core gene ac96 encodes a per os infectivity factor (PIF-4)
    • Fang, M., Y. Nie, S. Harris, M. A. Erlandson, and D. A. Theilmann. 2009. Autographa californica multiple nucleopolyhedrovirus core gene ac96 encodes a per os infectivity factor (PIF-4). J. Virol. 83:12569-12578.
    • (2009) J. Virol. , vol.83 , pp. 12569-12578
    • Fang, M.1    Nie, Y.2    Harris, S.3    Erlandson, M.A.4    Theilmann, D.A.5
  • 10
    • 0022629062 scopus 로고
    • Further characterization of an alkaline protease activity associated with iridescent virus type 6
    • Farara, T., and J. Attias. 1986. Further characterization of an alkaline protease activity associated with iridescent virus type 6. Brief report. Arch. Virol. 87:307-314.
    • (1986) Brief report. Arch. Virol. , vol.87 , pp. 307-314
    • Farara, T.1    Attias, J.2
  • 11
    • 0030728639 scopus 로고    scopus 로고
    • Analysis of P74, a PDV envelope protein of Autographa californica nucleopolyhedrovirus required for occlusion body infectivity in vivo
    • Faulkner, P., J. Kuzio, G. V. Williams, and J. A. Wilson. 1997. Analysis of P74, a PDV envelope protein of Autographa californica nucleopolyhedrovirus required for occlusion body infectivity in vivo. J. Gen. Virol. 78:3091-3100.
    • (1997) J. Gen. Virol. , vol.78 , pp. 3091-3100
    • Faulkner, P.1    Kuzio, J.2    Williams, G.V.3    Wilson, J.A.4
  • 12
    • 23144437891 scopus 로고    scopus 로고
    • DiANNA: a web server for disulfide connectivity prediction
    • Ferre, F., and P. Clote. 2005. DiANNA: a web server for disulfide connectivity prediction. Nucleic Acids Res. 33:W230-W232.
    • (2005) Nucleic Acids Res , vol.33
    • Ferre, F.1    Clote, P.2
  • 13
    • 0035864294 scopus 로고    scopus 로고
    • Coronavirus spike proteins in viral entry and pathogenesis
    • Gallagher, T. M., and M. J. Buchmeier. 2001. Coronavirus spike proteins in viral entry and pathogenesis. Virology 279:371-374.
    • (2001) Virology , vol.279 , pp. 371-374
    • Gallagher, T.M.1    Buchmeier, M.J.2
  • 14
    • 62749191549 scopus 로고    scopus 로고
    • Two viruses that cause salivary gland hypertrophy in Glossina pallidipes and Musca domestica are related and form a distinct phylogenetic clade
    • Garcia-Maruniak, A., et al. 2009. Two viruses that cause salivary gland hypertrophy in Glossina pallidipes and Musca domestica are related and form a distinct phylogenetic clade. J. Gen. Virol. 90:334-346.
    • (2009) J. Gen. Virol. , vol.90 , pp. 334-346
    • Garcia-Maruniak, A.1
  • 15
    • 38249040664 scopus 로고
    • Continuous cell line from Spodoptera exigua (Lepidoptera: Noctuidae) that supports replication of nuclear polyhedrosis viruses from Spodoptera exigua and Autographa californica
    • Gelernter, W. D., and B. A. Federici. 1986. Continuous cell line from Spodoptera exigua (Lepidoptera: Noctuidae) that supports replication of nuclear polyhedrosis viruses from Spodoptera exigua and Autographa californica. J. Invertebr. Pathol. 48:199-207.
    • (1986) J. Invertebr. Pathol. , vol.48 , pp. 199-207
    • Gelernter, W.D.1    Federici, B.A.2
  • 16
    • 2942676482 scopus 로고    scopus 로고
    • P74 mediates specific binding of Autographa californica M nucleopolyhedrovirus occlusion-derived virus to primary cellular targets in the midgut epithelia of Heliothis virescens larvae
    • Haas-Stapleton, E. J., J. O. Washburn, and L. E. Volkman. 2004. P74 mediates specific binding of Autographa californica M nucleopolyhedrovirus occlusion-derived virus to primary cellular targets in the midgut epithelia of Heliothis virescens larvae. J. Virol. 78:6786-6791.
    • (2004) J. Virol. , vol.78 , pp. 6786-6791
    • Haas-Stapleton, E.J.1    Washburn, J.O.2    Volkman, L.E.3
  • 17
    • 77951070087 scopus 로고    scopus 로고
    • Autographa californica multiple nucleopolyhedrovirus ODV-E56 envelope protein is required for oral infectivity and can be substituted functionally by Rachiplusia ou multiple nucleopolyhedrovirus ODV-E56
    • Harrison, R. L., W. O. Sparks, and B. C. Bonning. 2010. Autographa californica multiple nucleopolyhedrovirus ODV-E56 envelope protein is required for oral infectivity and can be substituted functionally by Rachiplusia ou multiple nucleopolyhedrovirus ODV-E56. J. Gen. Virol. 91:1173-1182.
    • (2010) J. Gen. Virol. , vol.91 , pp. 1173-1182
    • Harrison, R.L.1    Sparks, W.O.2    Bonning, B.C.3
  • 18
    • 0026344308 scopus 로고
    • (HX)n repeats: a pH-controlled protein-protein interaction motif of eukaryotic transcription factors?
    • Janknecht, R., C. Sander, and O. Pongs. 1991. (HX)n repeats: a pH-controlled protein-protein interaction motif of eukaryotic transcription factors? FEBS Lett. 295:1-2.
    • (1991) FEBS Lett , vol.295 , pp. 1-2
    • Janknecht, R.1    Sander, C.2    Pongs, O.3
  • 19
    • 0036936659 scopus 로고    scopus 로고
    • Characterization of pif, a gene required for the per os infectivity of Spodoptera littoralis nucleopolyhedrovirus
    • Kikhno, I., S. Gutierrez, L. Croizier, G. Croizier, and M. L. Ferber. 2002. Characterization of pif, a gene required for the per os infectivity of Spodoptera littoralis nucleopolyhedrovirus. J. Gen. Virol. 83:3013-3022.
    • (2002) J. Gen. Virol. , vol.83 , pp. 3013-3022
    • Kikhno, I.1    Gutierrez, S.2    Croizier, L.3    Croizier, G.4    Ferber, M.L.5
  • 20
    • 0016640964 scopus 로고
    • Proteolytic cleavage of polyhedral protein during dissolution of inclusion bodies of the nuclear polyhedrosis viruses of Bombyx mori and Galleria mellonella under alkaline conditions
    • Kozlov, E. A., N. M. Sidorova, and S. B. Serebryani. 1975. Proteolytic cleavage of polyhedral protein during dissolution of inclusion bodies of the nuclear polyhedrosis viruses of Bombyx mori and Galleria mellonella under alkaline conditions. J. Invertebr. Pathol. 25:97-101.
    • (1975) J. Invertebr. Pathol. , vol.25 , pp. 97-101
    • Kozlov, E.A.1    Sidorova, N.M.2    Serebryani, S.B.3
  • 21
    • 0019449946 scopus 로고
    • Protease activity associated with the capsule protein of Estigmene acres granulosis virus
    • Langridge, W. H., and K. Balter. 1981. Protease activity associated with the capsule protein of Estigmene acres granulosis virus. Virology 114:595-600.
    • (1981) Virology , vol.114 , pp. 595-600
    • Langridge, W.H.1    Balter, K.2
  • 22
    • 0030587958 scopus 로고    scopus 로고
    • Isolation from human placenta of the IgG transporter, FcRn, and localization to the syncytiotrophoblast: implications for maternal-fetal antibody transport
    • Leach, J. L., et al. 1996. Isolation from human placenta of the IgG transporter, FcRn, and localization to the syncytiotrophoblast: implications for maternal-fetal antibody transport. J. Immunol. 157:3317-3322.
    • (1996) J. Immunol. , vol.157 , pp. 3317-3322
    • Leach, J.L.1
  • 23
    • 29744458156 scopus 로고    scopus 로고
    • Specific binding of Autographa californica M nucleopolyhedrovirus occlusion-derived virus to midgut cells of Heliothis virescens larvae is mediated by products of pif genes Ac119 and Ac022 but not by Ac115
    • Ohkawa, T., J. O. Washburn, R. Sitapara, E. Sid, and L. E. Volkman. 2005. Specific binding of Autographa californica M nucleopolyhedrovirus occlusion-derived virus to midgut cells of Heliothis virescens larvae is mediated by products of pif genes Ac119 and Ac022 but not by Ac115. J. Virol. 79:15258-15264.
    • (2005) J. Virol. , vol.79 , pp. 15258-15264
    • Ohkawa, T.1    Washburn, J.O.2    Sitapara, R.3    Sid, E.4    Volkman, L.E.5
  • 24
    • 75749133275 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility
    • Pancera, M., et al. 2010. Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility. Proc. Natl. Acad. Sci. U. S. A. 107:1166-1171.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 1166-1171
    • Pancera, M.1
  • 25
    • 0017872732 scopus 로고
    • Alkaline protease associated with virus particles of a nuclear polyhedrosis virus: assay, purification, and properties
    • Payne, C. C., and J. Kalmakoff. 1978. Alkaline protease associated with virus particles of a nuclear polyhedrosis virus: assay, purification, and properties. J. Virol. 26:84-92.
    • (1978) J. Virol. , vol.26 , pp. 84-92
    • Payne, C.C.1    Kalmakoff, J.2
  • 26
    • 77956024384 scopus 로고    scopus 로고
    • Baculovirus per os infectivity factors form a complex on the surface of occlusion-derived virus
    • Peng, K., M. M. van Oers, Z. Hu, J. W. van Lent, and J. M. Vlak. 2010. Baculovirus per os infectivity factors form a complex on the surface of occlusion-derived virus. J. Virol. 84:9497-9504.
    • (2010) J. Virol. , vol.84 , pp. 9497-9504
    • Peng, K.1    van Oers, M.M.2    Hu, Z.3    van Lent, J.W.4    Vlak, J.M.5
  • 27
    • 76849098011 scopus 로고    scopus 로고
    • Identification of protein-protein interactions of the occlusion-derived virus-associated proteins of Helicoverpa armigera nucleopolyhedrovirus
    • Peng, K., et al. 2010. Identification of protein-protein interactions of the occlusion-derived virus-associated proteins of Helicoverpa armigera nucleopolyhedrovirus. J. Gen. Virol. 91:659-670.
    • (2010) J. Gen. Virol. , vol.91 , pp. 659-670
    • Peng, K.1
  • 28
    • 0042668524 scopus 로고    scopus 로고
    • Identification of pif-2, a third conserved baculovirus gene required for per os infection of insects
    • Pijlman, G. P., A. J. Pruijssers, and J. M. Vlak. 2003. Identification of pif-2, a third conserved baculovirus gene required for per os infection of insects. J. Gen. Virol. 84:2041-2049.
    • (2003) J. Gen. Virol. , vol.84 , pp. 2041-2049
    • Pijlman, G.P.1    Pruijssers, A.J.2    Vlak, J.M.3
  • 29
    • 48249148222 scopus 로고    scopus 로고
    • Dependence of antibody-mediated presentation of antigen on FcRn
    • Qiao, S. W., et al. 2008. Dependence of antibody-mediated presentation of antigen on FcRn. Proc. Natl. Acad. Sci. U. S. A. 105:9337-9342.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 9337-9342
    • Qiao, S.W.1
  • 30
    • 65549134398 scopus 로고    scopus 로고
    • National Library of Medicine, National Center for Biotechnology Information, Bethesda, MD
    • Rohrmann, G. F. 2010. Baculovirus molecular biology. National Library of Medicine, National Center for Biotechnology Information, Bethesda, MD.
    • (2010) Baculovirus molecular biology
    • Rohrmann, G.F.1
  • 31
    • 23844448345 scopus 로고    scopus 로고
    • Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry
    • Simmons, G., et al. 2005. Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry. Proc. Natl. Acad. Sci. U. S. A. 102:11876-11881.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 11876-11881
    • Simmons, G.1
  • 32
    • 33845979502 scopus 로고    scopus 로고
    • The baculoviruses occlusion-derived virus: virion structure and function
    • Slack, J., and B. M. Arif. 2007. The baculoviruses occlusion-derived virus: virion structure and function. Adv. Virus Res. 69:99-165.
    • (2007) Adv. Virus Res. , vol.69 , pp. 99-165
    • Slack, J.1    Arif, B.M.2
  • 33
    • 20044380569 scopus 로고    scopus 로고
    • Evidence for proteolytic cleavage of the baculovirus occlusion-derived virion envelope protein P74
    • Slack, J. M., and S. D. Lawrence. 2005. Evidence for proteolytic cleavage of the baculovirus occlusion-derived virion envelope protein P74. J. Gen. Virol. 86:1637-1643.
    • (2005) J. Gen. Virol. , vol.86 , pp. 1637-1643
    • Slack, J.M.1    Lawrence, S.D.2
  • 34
    • 54449086439 scopus 로고    scopus 로고
    • Trypsin cleavage of the baculovirus occlusion-derived virus attachment protein P74 is prerequisite in per os infection
    • Slack, J. M., S. D. Lawrence, P. J. Krell, and B. M. Arif. 2008. Trypsin cleavage of the baculovirus occlusion-derived virus attachment protein P74 is prerequisite in per os infection. J. Gen. Virol. 89:2388-2397.
    • (2008) J. Gen. Virol. , vol.89 , pp. 2388-2397
    • Slack, J.M.1    Lawrence, S.D.2    Krell, P.J.3    Arif, B.M.4
  • 35
    • 71949123985 scopus 로고    scopus 로고
    • Viral entry mechanisms: the increasing diversity of paramyxovirus entry
    • Smith, E. C., A. Popa, A. Chang, C. Masante, and R. E. Dutch. 2009. Viral entry mechanisms: the increasing diversity of paramyxovirus entry. FEBS J. 276:7217-7227.
    • (2009) FEBS J , vol.276 , pp. 7217-7227
    • Smith, E.C.1    Popa, A.2    Chang, A.3    Masante, C.4    Dutch, R.E.5
  • 36
    • 1842639396 scopus 로고    scopus 로고
    • pH dependence and stoichiometry of binding to the Fc region of IgG by the herpes simplex virus Fc receptor gE-gI
    • Sprague, E. R., W. L. Martin, and P. J. Bjorkman. 2004. pH dependence and stoichiometry of binding to the Fc region of IgG by the herpes simplex virus Fc receptor gE-gI. J. Biol. Chem. 279:14184-14193.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14184-14193
    • Sprague, E.R.1    Martin, W.L.2    Bjorkman, P.J.3
  • 37
    • 0033602713 scopus 로고    scopus 로고
    • Role of hemagglutinin cleavage for the pathogenicity of influenza virus
    • Steinhauer, D. A. 1999. Role of hemagglutinin cleavage for the pathogenicity of influenza virus. Virology 258:1-20.
    • (1999) Virology , vol.258 , pp. 1-20
    • Steinhauer, D.A.1
  • 38
    • 0016686033 scopus 로고
    • Trichoplusia ni granulosis virus granulin: a phenol-soluble, phosphorylated protein
    • Summers, M. D., and G. E. Smith. 1975. Trichoplusia ni granulosis virus granulin: a phenol-soluble, phosphorylated protein. J. Virol. 16:1108-1116.
    • (1975) J. Virol. , vol.16 , pp. 1108-1116
    • Summers, M.D.1    Smith, G.E.2
  • 39
    • 0017979744 scopus 로고
    • Characterization of an alkaline protease associated with a granulosis virus of Plodia interpunctella
    • Tweeten, K. A., L. A. Bulla, Jr., and R. A. Consigli. 1978. Characterization of an alkaline protease associated with a granulosis virus of Plodia interpunctella. J. Virol. 26:703-711.
    • (1978) J. Virol. , vol.26 , pp. 703-711
    • Tweeten, K.A.1    Bulla Jr., L.A.2    Consigli, R.A.3
  • 40
    • 0015901099 scopus 로고
    • Replication and infectivity of the nuclear polyhedrosis virus of the alfalfa looper, Autographa californica, produced in cells grown in vitro
    • Vail, P. V., D. L. Jay, and W. F. Hink. 1973. Replication and infectivity of the nuclear polyhedrosis virus of the alfalfa looper, Autographa californica, produced in cells grown in vitro. J. Invertebr. Pathol. 22:231-237.
    • (1973) J. Invertebr. Pathol. , vol.22 , pp. 231-237
    • Vail, P.V.1    Jay, D.L.2    Hink, W.F.3
  • 41
    • 79959718203 scopus 로고    scopus 로고
    • The genome of Oryctes rhinoceros nudivirus provides novel insight into the evolution of nuclear arthropod-specific large circular doublestranded DNA viruses
    • Wang, Y., O. R. Bininda-Emonds, M. M. van Oers, J. M. Vlak, and J. A. Jehle. 2011. The genome of Oryctes rhinoceros nudivirus provides novel insight into the evolution of nuclear arthropod-specific large circular doublestranded DNA viruses. Virus Genes 42:444-456.
    • (2011) Virus Genes , vol.42 , pp. 444-456
    • Wang, Y.1    Bininda-Emonds, O.R.2    van Oers, M.M.3    Vlak, J.M.4    Jehle, J.A.5
  • 42
    • 67649908431 scopus 로고    scopus 로고
    • Nudiviruses and other large, doublestranded circular DNA viruses of invertebrates: new insights on an old topic
    • Wang, Y., and J. A. Jehle. 2009. Nudiviruses and other large, doublestranded circular DNA viruses of invertebrates: new insights on an old topic. J. Invertebr. Pathol. 101:187-193.
    • (2009) J. Invertebr. Pathol. , vol.101 , pp. 187-193
    • Wang, Y.1    Jehle, J.A.2
  • 43
    • 0036133063 scopus 로고    scopus 로고
    • Furin is involved in baculovirus envelope fusion protein activation
    • Westenberg, M., et al. 2002. Furin is involved in baculovirus envelope fusion protein activation. J. Virol. 76:178-184.
    • (2002) J. Virol. , vol.76 , pp. 178-184
    • Westenberg, M.1
  • 44
    • 0018897583 scopus 로고
    • Protease degradation of Autographa californica nuclear polyhedrosis virus proteins
    • Wood, H. A. 1980. Protease degradation of Autographa californica nuclear polyhedrosis virus proteins. Virology 103:392-399.
    • (1980) Virology , vol.103 , pp. 392-399
    • Wood, H.A.1


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