메뉴 건너뛰기




Volumn 74, Issue 14, 2000, Pages 6546-6555

Trypsin-induced structural transformation in aquareovirus

Author keywords

[No Author keywords available]

Indexed keywords

TRYPSIN;

EID: 0033919812     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.74.14.6546-6555.2000     Document Type: Article
Times cited : (50)

References (37)
  • 1
    • 0006972583 scopus 로고
    • Association of a Moraxella sp. and reo-like virus with mortalities of striped bass, Marone saxatilis
    • F. Perkins and T. Cheng (ed.). Academic Press, Inc., New York, N.Y.
    • Baya, A., A. E. Toranzo, S. Nunez, J. L. Barja, and F. M. Hetrick. 1990. Association of a Moraxella sp. and reo-like virus with mortalities of striped bass, Marone saxatilis, p. 91-99. In F. Perkins and T. Cheng (ed.), Pathology in marine science. Academic Press, Inc., New York, N.Y.
    • (1990) Pathology in Marine Science , pp. 91-99
    • Baya, A.1    Toranzo, A.E.2    Nunez, S.3    Barja, J.L.4    Hetrick, F.M.5
  • 2
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther, R. A. 1971. Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Philos. Trans. R. Soc. London Ser B. 261:221-230.
    • (1971) Philos. Trans. R. Soc. London Ser B. , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 3
    • 0025049962 scopus 로고
    • A sigma 1 region important for hemagglutination by serotype 3 reovirus strains
    • Dermody, T. S., M. L. Nibert, R. Bassel-Duby, and B. N. Fields. 1990. A sigma 1 region important for hemagglutination by serotype 3 reovirus strains. J. Virol. 64:5173-5176.
    • (1990) J. Virol. , vol.64 , pp. 5173-5176
    • Dermody, T.S.1    Nibert, M.L.2    Bassel-Duby, R.3    Fields, B.N.4
  • 4
    • 0032565725 scopus 로고    scopus 로고
    • Internal/structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus
    • Dryden, K. A., D. L. Farsetta, G. Wang, J. M. Keegan, B. N. Fields, T. S. Baker, and M. L. Nibert. 1998. Internal/structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus. Virology 245:33-46.
    • (1998) Virology , vol.245 , pp. 33-46
    • Dryden, K.A.1    Farsetta, D.L.2    Wang, G.3    Keegan, J.M.4    Fields, B.N.5    Baker, T.S.6    Nibert, M.L.7
  • 5
    • 0027162058 scopus 로고
    • Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: Analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction
    • Dryden, K. A., G. Wang, M. Yeager, M. L. Nibert, K. M. Coombs, D. B. Furlong, B. N. Fields, and T. S. Baker. 1993. Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction. J. Cell Biol. 122:1023-1041.
    • (1993) J. Cell Biol. , vol.122 , pp. 1023-1041
    • Dryden, K.A.1    Wang, G.2    Yeager, M.3    Nibert, M.L.4    Coombs, K.M.5    Furlong, D.B.6    Fields, B.N.7    Baker, T.S.8
  • 7
    • 0019440664 scopus 로고
    • Proteolytic enhancement of rotavirus infectivity: Molecular mechanisms
    • Estes, M. K., D. Y. Graham, and B. B. Mason. 1981. Proteolytic enhancement of rotavirus infectivity: molecular mechanisms. J. Virol. 39:879-888.
    • (1981) J. Virol. , vol.39 , pp. 879-888
    • Estes, M.K.1    Graham, D.Y.2    Mason, B.B.3
  • 8
    • 0023666171 scopus 로고
    • The T=4 envelope of sindbis virus is organized by interactions with a complementary T=3 capsid
    • Fuller, S. D. 1987. The T=4 envelope of Sindbis virus is organized by interactions with a complementary T=3 capsid. Cell 27:923-934.
    • (1987) Cell , vol.27 , pp. 923-934
    • Fuller, S.D.1
  • 11
    • 0015398520 scopus 로고
    • Studies on the effect of chymotrypsin on reovirions
    • Joklik, W. K. 1972. Studies on the effect of chymotrypsin on reovirions. Virology 49:700-715.
    • (1972) Virology , vol.49 , pp. 700-715
    • Joklik, W.K.1
  • 12
    • 0031031329 scopus 로고    scopus 로고
    • Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles
    • Lawton, J. A., M. K. Estes, and B. V. Prasad. 1997. Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles. Nat. Struct. Biol. 4:118-121.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 118-121
    • Lawton, J.A.1    Estes, M.K.2    Prasad, B.V.3
  • 13
    • 0029916491 scopus 로고    scopus 로고
    • Automated software package for icosahedral virus reconstruction
    • Lawton, J. A., and B. V. Venkataram Prasad. 1996. Automated software package for icosahedral virus reconstruction. J. Struct. Biol. 116:209-215.
    • (1996) J. Struct. Biol. , vol.116 , pp. 209-215
    • Lawton, J.A.1    Venkataram Prasad, B.V.2
  • 14
    • 0030768785 scopus 로고    scopus 로고
    • Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal-deleted VP2: Implications for the architecture of the VP2 capsid layer
    • Lawton, J. A., C. Q. Zeng, S. K. Mukherjee, J. Cohen, M. K. Estes, and B. V. Prasad. 1997. Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal-deleted VP2: implications for the architecture of the VP2 capsid layer. J. Virol. 71:7353-7360.
    • (1997) J. Virol. , vol.71 , pp. 7353-7360
    • Lawton, J.A.1    Zeng, C.Q.2    Mukherjee, S.K.3    Cohen, J.4    Estes, M.K.5    Prasad, B.V.6
  • 15
    • 0019522275 scopus 로고
    • Protein sigma 1 is the reovirus cell attachment protein
    • Lee, P. W. K., E. C. Hayes, and W. K. Joklik. 1981. Protein sigma 1 is the reovirus cell attachment protein. Virology 108:156-163.
    • (1981) Virology , vol.108 , pp. 156-163
    • Lee, P.W.K.1    Hayes, E.C.2    Joklik, W.K.3
  • 17
    • 0030950333 scopus 로고    scopus 로고
    • Cloning, sequence analysis and expression of the major outer capsid protein gene of an aquareovirus
    • Lupiani, B., S. M. Reddy, K. Subramanian, and S. K. Samal. 1997. Cloning, sequence analysis and expression of the major outer capsid protein gene of an aquareovirus. J. Gen. Virol. 78:1379-1383.
    • (1997) J. Gen. Virol. , vol.78 , pp. 1379-1383
    • Lupiani, B.1    Reddy, S.M.2    Subramanian, K.3    Samal, S.K.4
  • 19
    • 0031901462 scopus 로고    scopus 로고
    • Enhancement of aquareovirus infectivity by treatment with proteases: Mechanism of action
    • McPhillips, T. H., D. Dinan, K. Subramanian, and S. K. Samal. 1998. Enhancement of aquareovirus infectivity by treatment with proteases: mechanism of action. J. Virol. 72:3387-3389.
    • (1998) J. Virol. , vol.72 , pp. 3387-3389
    • McPhillips, T.H.1    Dinan, D.2    Subramanian, K.3    Samal, S.K.4
  • 20
    • 0029927461 scopus 로고    scopus 로고
    • Enhanced infectivity of modified bluetongue virus particles for two insect cell lines and for two Culicoides vector species
    • Mertens, P. P. C, J. N. Burroughs, A. Walton, M. P. Wellby, H. Fu, R. S. O'Hara, S. M. Brookes, and P. S. Mellor. 1996. Enhanced infectivity of modified bluetongue virus particles for two insect cell lines and for two Culicoides vector species. Virology 217:582-593.
    • (1996) Virology , vol.217 , pp. 582-593
    • Mertens, P.P.C.1    Burroughs, J.N.2    Walton, A.3    Wellby, M.P.4    Fu, H.5    O'Hara, R.S.6    Brookes, S.M.7    Mellor, P.S.8
  • 21
    • 0031950354 scopus 로고    scopus 로고
    • Structure of mammalian orthoreovirus particles
    • K. Tyler and M. Oldstone (ed.). Springer-Verlag KG, Berlin, Germany
    • Nibert, M. L. 1998. Structure of mammalian orthoreovirus particles, p. 1-30. In K. Tyler and M. Oldstone (ed.), Structure, proteins, and genetics, vol. 1. Springer-Verlag KG, Berlin, Germany.
    • (1998) Structure, Proteins, and Genetics , vol.1 , pp. 1-30
    • Nibert, M.L.1
  • 22
    • 0029058860 scopus 로고
    • Infectious subvirion particles of reovirus type 3 Dearing exhibit a loss in infectivity and contain a cleaved sigma 1 protein
    • Nilbert, M. L., J. D. Chappell, and T. S. Dermody. 1995. Infectious subvirion particles of reovirus type 3 Dearing exhibit a loss in infectivity and contain a cleaved sigma 1 protein. J. Virol. 69:5057-5067.
    • (1995) J. Virol. , vol.69 , pp. 5057-5067
    • Nilbert, M.L.1    Chappell, J.D.2    Dermody, T.S.3
  • 23
    • 0026733619 scopus 로고
    • A carboxy-terminal fragment of protein mu 1/mu 1C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetration
    • Nibert, M. L., and B. N. Fields. 1992. A carboxy-terminal fragment of protein mu 1/mu 1C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetration. J. Virol. 66:6408-6418.
    • (1992) J. Virol. , vol.66 , pp. 6408-6418
    • Nibert, M.L.1    Fields, B.N.2
  • 24
    • 0029839752 scopus 로고    scopus 로고
    • Visualization of ordered genomic RNA and localization of transcriptional complexes in rotavirus
    • Prasad, B. V., R. Rothnagel, C. Q. Zeng, J. Jakana, J. A. Lawton, W. Chiu, and M. K. Estes. 1996. Visualization of ordered genomic RNA and localization of transcriptional complexes in rotavirus. Nature 382:471-473.
    • (1996) Nature , vol.382 , pp. 471-473
    • Prasad, B.V.1    Rothnagel, R.2    Zeng, C.Q.3    Jakana, J.4    Lawton, J.A.5    Chiu, W.6    Estes, M.K.7
  • 25
    • 0001829831 scopus 로고    scopus 로고
    • Molecular basis of rotavirus replication
    • W. Chiu and R. Burnett and R. Garcea (ed.). Oxford University Press, New York, N.Y.
    • Prasad, B. V. V., and M. K. Estes. 1997. Molecular basis of rotavirus replication, p. 239-268. In W. Chiu and R. Burnett and R. Garcea (ed.), Structural biology of viruses. Oxford University Press, New York, N.Y.
    • (1997) Structural Biology of Viruses , pp. 239-268
    • Prasad, B.V.V.1    Estes, M.K.2
  • 26
    • 0034720237 scopus 로고    scopus 로고
    • Structure of the reovirus core at 3.6 Å resolution
    • Reinisch, K., M. L. Nibert, and S. Harrison. 2000. Structure of the reovirus core at 3.6 Å resolution. Nature 404:960-967.
    • (2000) Nature , vol.404 , pp. 960-967
    • Reinisch, K.1    Nibert, M.L.2    Harrison, S.3
  • 27
    • 0002992717 scopus 로고    scopus 로고
    • Orbiviruses and their replication
    • B. Fields, D. Knipe, and P. Howley (ed.). Lippincott-Raven, Philadelphia, Pa.
    • Roy, P. 1996. Orbiviruses and their replication, p. 1709-1766. In B. Fields, D. Knipe, and P. Howley (ed.), Fields virology, 3rd ed., vol. 2. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , vol.2 , pp. 1709-1766
    • Roy, P.1
  • 28
    • 0025173021 scopus 로고
    • Molecular characterization of a rotaviruslike virus isolated from striped bass (Morone saxatilis)
    • Samal, S. K., C. P. Dopazo, T. H. McPhillips, A. Baya, S. B. Mohanty, and F. M. Hetrick. 1990. Molecular characterization of a rotaviruslike virus isolated from striped bass (Morone saxatilis). J. Virol. 64:5235-5240.
    • (1990) J. Virol. , vol.64 , pp. 5235-5240
    • Samal, S.K.1    Dopazo, C.P.2    McPhillips, T.H.3    Baya, A.4    Mohanty, S.B.5    Hetrick, F.M.6
  • 29
    • 0030586878 scopus 로고    scopus 로고
    • The structure of aquareovirus shows how the different geometries of the two layers of the capsid are reconciled to provide symmetrical interactions and stabilization
    • Shaw, A. L., S. K. Samal, K. Subramanlan, and B. V. Prasad. 1996. The structure of aquareovirus shows how the different geometries of the two layers of the capsid are reconciled to provide symmetrical interactions and stabilization. Structure 4:957-967.
    • (1996) Structure , vol.4 , pp. 957-967
    • Shaw, A.L.1    Samal, S.K.2    Subramanlan, K.3    Prasad, B.V.4
  • 30
    • 0027949185 scopus 로고
    • Characterization of the polypeptides and determination of genome coding assignments of an aquareovirus
    • Subramanian, K., T. H. McPhillips, and S. K. Samal. 1994. Characterization of the polypeptides and determination of genome coding assignments of an aquareovirus. Virology 205:75-81.
    • (1994) Virology , vol.205 , pp. 75-81
    • Subramanian, K.1    McPhillips, T.H.2    Samal, S.K.3
  • 31
    • 0023090371 scopus 로고
    • Similarity measures between images
    • van Heel, M. 1987. Similarity measures between images. Ultramicroscopy 21:95-99.
    • (1987) Ultramicroscopy , vol.21 , pp. 95-99
    • Van Heel, M.1
  • 32
    • 0017295002 scopus 로고
    • Studies on the structure of reovirus cores: Selective removal of polypeptide lambda 2
    • White, C. K., and H. J. Zweerink. 1976. Studies on the structure of reovirus cores: selective removal of polypeptide lambda 2. Virology 70:171-180.
    • (1976) Virology , vol.70 , pp. 171-180
    • White, C.K.1    Zweerink, H.J.2
  • 33
    • 0001506192 scopus 로고
    • Isolation of a new reovirus from chum salmon in Japan
    • Winton, J. R., C. N. Lannan, J. L. Fryer, and T. Kimura. 1981. Isolation of a new reovirus from chum salmon in Japan. Fish Pathol. 15:155-162.
    • (1981) Fish Pathol. , vol.15 , pp. 155-162
    • Winton, J.R.1    Lannan, C.N.2    Fryer, J.L.3    Kimura, T.4
  • 34
    • 0000234954 scopus 로고    scopus 로고
    • Transcriptionally active reovirus core particles visualized by electron cryo-microscopy and image reconstruction
    • Yeager, M., S. Weiner, and K. M. Coombs. 1996. Transcriptionally active reovirus core particles visualized by electron cryo-microscopy and image reconstruction. Biophys. J. 70:A116.
    • (1996) Biophys. J. , vol.70
    • Yeager, M.1    Weiner, S.2    Coombs, K.M.3
  • 35
    • 0030030595 scopus 로고    scopus 로고
    • The M1 gene is associated with differences in the temperature optimum of the transcriptase activity in reovirus core particles
    • Yin, P., M. Cheang, and K. M. Coombs. 1996. The M1 gene is associated with differences in the temperature optimum of the transcriptase activity in reovirus core particles. J. Virol. 70:1223-1227.
    • (1996) J. Virol. , vol.70 , pp. 1223-1227
    • Yin, P.1    Cheang, M.2    Coombs, K.M.3
  • 37
    • 0028151168 scopus 로고
    • Protein subunit structures in the herpes simplex virus A-capsid determined from 400 kV spot-scan electron cryomicroscopy
    • Zhou, Z. H., B. V. V. Prasad, J. Jakana, F. J. Rixon, and W. Chiu. 1994. Protein subunit structures in the herpes simplex virus A-capsid determined from 400 kV spot-scan electron cryomicroscopy. J. Mol. Biol. 242:456-469.
    • (1994) J. Mol. Biol. , vol.242 , pp. 456-469
    • Zhou, Z.H.1    Prasad, B.V.V.2    Jakana, J.3    Rixon, F.J.4    Chiu, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.