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Volumn 84, Issue 4, 2003, Pages 863-873

Identification and analysis of gp116 and gp64 structural glycoproteins of yellow head nidovirus of Penaeus monodon shrimp

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; LEUCINE; NITROGEN; OXYGEN; POLYPEPTIDE; POLYPROTEIN; PROTEIN ANTIBODY; RECOMBINANT PROTEIN; STRUCTURAL PROTEIN; THREONINE; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; VIRUS GLYCOPROTEIN GP 116; VIRUS GLYCOPROTEIN GP 64;

EID: 0037385667     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/vir.0.18811-0     Document Type: Review
Times cited : (58)

References (38)
  • 2
    • 0021915773 scopus 로고
    • Cloning and sequencing of the gene encoding the spike protein of the coronavirus IBV
    • Binns, M. M., Boursnell, M. E. G., Cavanagh, D., Pappin, D. J. C. & Brown, T. D. (1985). Cloning and sequencing of the gene encoding the spike protein of the coronavirus IBV. J Gen Virol 66, 719-727.
    • (1985) J. Gen. Virol. , vol.66 , pp. 719-727
    • Binns, M.M.1    Boursnell, M.E.G.2    Cavanagh, D.3    Pappin, D.J.C.4    Brown, T.D.5
  • 3
    • 0026415343 scopus 로고
    • Coronavirus motif
    • Britton, P. (1991). Coronavirus motif. Nature 353, 394.
    • (1991) Nature , vol.353 , pp. 394
    • Britton, P.1
  • 4
    • 0002437897 scopus 로고
    • The coronavirus surface glycoprotein
    • Edited by S. G. Siddell. New York: Plenum Press
    • Cavanagh, D. (1995). The coronavirus surface glycoprotein. In The Coronaviridae pp. 73-113. Edited by S. G. Siddell. New York: Plenum Press.
    • (1995) The Coronaviridae , pp. 73-113
    • Cavanagh, D.1
  • 6
    • 0036402693 scopus 로고    scopus 로고
    • The complete sequence of gill-associated virus of Penaeus monodon prawns indicates a gene organisation unique among nidoviruses
    • Cowley, J. A. & Walker, P. J. (2002). The complete sequence of gill-associated virus of Penaeus monodon prawns indicates a gene organisation unique among nidoviruses. Arch Virol 147, 1977-1987.
    • (2002) Arch. Virol. , vol.147 , pp. 1977-1987
    • Cowley, J.A.1    Walker, P.J.2
  • 7
    • 0033549144 scopus 로고    scopus 로고
    • Yellow head virus from Thailand and gill-associated virus from Australia are closely related but distinct prawn viruses
    • Cowley, J. A., Dimmock, C. M., Wongteerasupaya, C., Boonsaeng, V., Panyim, S. & Walker, P. J. (1999). Yellow head virus from Thailand and gill-associated virus from Australia are closely related but distinct prawn viruses. Dis Aquat Org 36, 153-157.
    • (1999) Dis. Aquat. Org. , vol.36 , pp. 153-157
    • Cowley, J.A.1    Dimmock, C.M.2    Wongteerasupaya, C.3    Boonsaeng, V.4    Panyim, S.5    Walker, P.J.6
  • 8
    • 0034093105 scopus 로고    scopus 로고
    • Gill-associated virus of Penaeus monodon prawns: An invertebrate nidovirus with ORF1a and ORF1b genes related to arteri- and coronaviruses
    • Cowley, J. A., Dimmock, C. M., Spann, K. M. & Walker, P. J. (2000). Gill-associated virus of Penaeus monodon prawns: an invertebrate nidovirus with ORF1a and ORF1b genes related to arteri- and coronaviruses. J Gen Virol 81, 1473-1484.
    • (2000) J. Gen. Virol. , vol.81 , pp. 1473-1484
    • Cowley, J.A.1    Dimmock, C.M.2    Spann, K.M.3    Walker, P.J.4
  • 9
    • 0035699442 scopus 로고    scopus 로고
    • Gill-associated virus of Penaeus monodon prawns: Molecular evidence for the first invertebrate nidovirus
    • Cowley, J. A., Dimmock, C. M., Spann, K. M. & Walker, P. J. (2001). Gill-associated virus of Penaeus monodon prawns: molecular evidence for the first invertebrate nidovirus. Advances in Experimental Medicine and Biology 494, 43-48.
    • (2001) Advances in Experimental Medicine and Biology , vol.494 , pp. 43-48
    • Cowley, J.A.1    Dimmock, C.M.2    Spann, K.M.3    Walker, P.J.4
  • 10
    • 0023430389 scopus 로고
    • cDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus
    • de Groot, R. J., Maduro, J., Lenstra, J. A., Horzinek, M. C., van der Zeijst, B. A. M. & Spaan, W. J. M. (1987a). cDNA cloning and sequence analysis of the gene encoding the peplomer protein of feline infectious peritonitis virus. J Gen Virol 68, 2639-2646.
    • (1987) J. Gen. Virol. , vol.68 , pp. 2639-2646
    • de Groot, R.J.1    Maduro, J.2    Lenstra, J.A.3    Horzinek, M.C.4    van der Zeijst, B.A.M.5    Spaan, W.J.M.6
  • 12
    • 0031637565 scopus 로고    scopus 로고
    • Raising polyclonal antibodies using nitrocellulose-bound antigen
    • Diano, M., Le Bivic, A. & Hirn, M. (1998). Raising polyclonal antibodies using nitrocellulose-bound antigen. Methods Mol Biol 80, 5-13.
    • (1998) Methods Mol. Biol. , vol.80 , pp. 5-13
    • Diano, M.1    Le Bivic, A.2    Hirn, M.3
  • 13
    • 0028326371 scopus 로고
    • Sequence of the spike protein of the porcine epidemic diarrhoea virus
    • Duarte, M. & Laude, H. (1994). Sequence of the spike protein of the porcine epidemic diarrhoea virus. J Gen Virol 75, 1195-1200.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1195-1200
    • Duarte, M.1    Laude, H.2
  • 15
    • 0030835811 scopus 로고    scopus 로고
    • Major viral diseases of the black tiger prawn (Penaeus monodon) in Thailand
    • Flegel, T. W. (1997). Major viral diseases of the black tiger prawn (Penaeus monodon) in Thailand. World J Microbiol Biotechnol 13, 433-442.
    • (1997) World J. Microbiol. Biotechnol. , vol.13 , pp. 433-442
    • Flegel, T.W.1
  • 16
    • 0028133455 scopus 로고
    • Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1-specific monoclonal antibody
    • Grosse, B. & Siddell, S. G. (1994). Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1-specific monoclonal antibody. Virology 202, 814-824.
    • (1994) Virology , vol.202 , pp. 814-824
    • Grosse, B.1    Siddell, S.G.2
  • 17
    • 0030860232 scopus 로고    scopus 로고
    • O-GLYCBASE version 2.0 - A revised database of O-glycosylated proteins
    • Hansen, J. E., Lund, O., Rapacki, K. & Brunak, S. (1997). O-GLYCBASE version 2.0 - a revised database of O-glycosylated proteins. Nucleic Acids Res 25, 278-282.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 278-282
    • Hansen, J.E.1    Lund, O.2    Rapacki, K.3    Brunak, S.4
  • 18
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Laarsson, B., von Heijne, G. & Sonnhammer, E. L. L. (2001). Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 305, 567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Laarsson, B.2    von Heijne, G.3    Sonnhammer, E.L.L.4
  • 19
    • 0028018126 scopus 로고
    • Localization of neutralization epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein
    • Kubo, H., Yamada, Y. K. & Taguchi, F. (1994). Localization of neutralization epitopes and the receptor-binding site within the amino-terminal 330 amino acids of the murine coronavirus spike protein. J Virol 68, 5403-5410.
    • (1994) J. Virol. , vol.68 , pp. 5403-5410
    • Kubo, H.1    Yamada, Y.K.2    Taguchi, F.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0032827589 scopus 로고    scopus 로고
    • Amino acid substitutions within the leucine zipper domain of the murine coronavirus spike protein cause defects in oligomerization and the ability to induce cell-to-cell fusion
    • Luo, Z., Matthews, A. M. & Weiss, S. R. (1999). Amino acid substitutions within the leucine zipper domain of the murine coronavirus spike protein cause defects in oligomerization and the ability to induce cell-to-cell fusion. J Virol 73, 8152-8159.
    • (1999) J. Virol. , vol.73 , pp. 8152-8159
    • Luo, Z.1    Matthews, A.M.2    Weiss, S.R.3
  • 24
    • 0027208602 scopus 로고
    • Molecular characterization of the S protein gene of human coronavirus OC43
    • Mounir, S. & Talbot, P. (1993). Molecular characterization of the S protein gene of human coronavirus OC43. J Gen Virol 74, 1981-1987.
    • (1993) J. Gen. Virol. , vol.74 , pp. 1981-1987
    • Mounir, S.1    Talbot, P.2
  • 25
    • 0024969849 scopus 로고
    • Modification of sialyl residue of glycoconjugates by reductive amination: Characterization of the modified sialic acids
    • Murray, M. C., Bhavanadan, V. P. & Davidson, E. E. (1989). Modification of sialyl residue of glycoconjugates by reductive amination: characterization of the modified sialic acids. Carbohydr Res 186, 255-265.
    • (1989) Carbohydr. Res. , vol.186 , pp. 255-265
    • Murray, M.C.1    Bhavanadan, V.P.2    Davidson, E.E.3
  • 26
    • 6844254536 scopus 로고    scopus 로고
    • Yellow-head virus: A rhabdovirus-like pathogen of penaeid shrimp
    • Nadala, E. C. B., Tappy, L. M. & Loh, P. C. (1997). Yellow-head virus: a rhabdovirus-like pathogen of penaeid shrimp. Dis Aquat Org 31, 141-146.
    • (1997) Dis. Aquat. Org. , vol.31 , pp. 141-146
    • Nadala, E.C.B.1    Tappy, L.M.2    Loh, P.C.3
  • 27
    • 0344500898 scopus 로고    scopus 로고
    • Pathogenesis of MHV4/MHV-A59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence
    • Phillips, J. J., Chua, M. M., Lavi, E. & Weiss, S. R. (1999). Pathogenesis of MHV4/MHV-A59 recombinant viruses: the murine coronavirus spike protein is a major determinant of neurovirulence. J Virol 73, 7752-7760.
    • (1999) J. Virol. , vol.73 , pp. 7752-7760
    • Phillips, J.J.1    Chua, M.M.2    Lavi, E.3    Weiss, S.R.4
  • 28
    • 0018640551 scopus 로고
    • Glycoprotein detection in polyacrylamide gel with thymol and sulfuric acid
    • Racusen, D. (1979). Glycoprotein detection in polyacrylamide gel with thymol and sulfuric acid. Anal Biochem 99, 474-476.
    • (1979) Anal. Biochem. , vol.99 , pp. 474-476
    • Racusen, D.1
  • 29
    • 0002753706 scopus 로고
    • The coronavirus membrane glycoprotein
    • Edited by S. G. Siddell. New York: Plenum Press
    • Rottier, P. J. M. (1995). The coronavirus membrane glycoprotein. In The Coronaviridae, pp. 115-139. Edited by S. G. Siddell. New York: Plenum Press.
    • (1995) The Coronaviridae , pp. 115-139
    • Rottier, P.J.M.1
  • 31
    • 0001903936 scopus 로고
    • The molecular biology of toroviruses
    • Edited by S. G. Siddell. New York: Plenum Press
    • Snijder, E. J. & Horzinek, M. C. (1995). The molecular biology of toroviruses. In The Coronaviridae, pp. 219-238. Edited by S. G. Siddell. New York: Plenum Press.
    • (1995) The Coronaviridae , pp. 219-238
    • Snijder, E.J.1    Horzinek, M.C.2
  • 32
    • 0024226792 scopus 로고
    • Coronavirus structure and genome expression
    • Spaan, W., Cavanagh, D. & Horzinek, M. C. (1988). Coronavirus structure and genome expression. J Gen Virol 69, 2939-2952.
    • (1988) J. Gen. Virol. , vol.69 , pp. 2939-2952
    • Spaan, W.1    Cavanagh, D.2    Horzinek, M.C.3
  • 33
    • 0022397327 scopus 로고
    • Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments
    • Sturman, L. S., Ricard, C. S. & Holmes, K. V. (1985). Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments. J Virol 56, 904-911.
    • (1985) J. Virol. , vol.56 , pp. 904-911
    • Sturman, L.S.1    Ricard, C.S.2    Holmes, K.V.3
  • 34
    • 0029918145 scopus 로고    scopus 로고
    • Analysis of the receptor binding site of murine coronavirus spike glycoprotein
    • Suzuki, H. & Taguchi, F. (1996). Analysis of the receptor binding site of murine coronavirus spike glycoprotein. J Virol 70, 2632-2636.
    • (1996) J. Virol. , vol.70 , pp. 2632-2636
    • Suzuki, H.1    Taguchi, F.2
  • 35
    • 0033605038 scopus 로고    scopus 로고
    • A yellow head virus probe: Application to in situ hybridization and determination of its nucleotide sequence
    • Tang, K. F.-J. & Lightner, D. V. (1998). A yellow head virus probe: application to in situ hybridization and determination of its nucleotide sequence. Dis Aquat Org 35, 165-173.
    • (1998) Dis. Aquat. Org. , vol.35 , pp. 165-173
    • Tang, K.F.-J.1    Lightner, D.V.2
  • 36
    • 0027968068 scopus 로고
    • CLUSTAL W: Improved sensitivity of the progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choices
    • Thompson, J. D., Higgins, D. G. & Gibson, T. L. (1994). CLUSTAL W: improved sensitivity of the progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choices. Nucleic Acids Res 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.L.3
  • 37
    • 0034421295 scopus 로고    scopus 로고
    • Yellow head virus infection in the giant tiger prawn Penaeus monodon cultured in Taiwan
    • Wang, Y.-C. & Chang, P.-S. (2000). Yellow head virus infection in the giant tiger prawn Penaeus monodon cultured in Taiwan. Fish Pathol 35, 1-10.
    • (2000) Fish Pathol. , vol.35 , pp. 1-10
    • Wang, Y.-C.1    Chang, P.-S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.