메뉴 건너뛰기




Volumn 71, Issue 8, 1997, Pages 6061-6067

Posttranslational processing and identification of a neutralization domain of the GP4 protein encoded by ORF4 of Lelystad virus

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS GLYCOPROTEIN;

EID: 0030837427     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.8.6061-6067.1997     Document Type: Article
Times cited : (95)

References (35)
  • 2
    • 0029833407 scopus 로고    scopus 로고
    • Structural polypeptides of the American (VR-2332) strain of porcine reproductive respiratory syndrome virus
    • Bautista, E. M., J. J. M. Meulenberg, C. S. Choi, and T. W. Molitor. 1996. Structural polypeptides of the American (VR-2332) strain of porcine reproductive respiratory syndrome virus. Arch. Virol. 141:1357-1365.
    • (1996) Arch. Virol. , vol.141 , pp. 1357-1365
    • Bautista, E.M.1    Meulenberg, J.J.M.2    Choi, C.S.3    Molitor, T.W.4
  • 5
    • 0027254342 scopus 로고
    • Molecular characterization of porcine reproductive and respiratory syndrome virus, a member of the Arterivirus group
    • Conzelmann, K. K., N. Visser, P. van Woensel, and H. J. Tiel. 1993. Molecular characterization of porcine reproductive and respiratory syndrome virus, a member of the Arterivirus group. Virology 193:329-339.
    • (1993) Virology , vol.193 , pp. 329-339
    • Conzelmann, K.K.1    Visser, N.2    Van Woensel, P.3    Tiel, H.J.4
  • 9
    • 0028969720 scopus 로고
    • Disulfide bonds between two envelope proteins of lactate dehydrogenase-elevating virus are essential for viral infectivity
    • Faaberg, K. S., C. Even, G. A. Palmer, and P. G. W. Plagemann. 1995. Disulfide bonds between two envelope proteins of lactate dehydrogenase-elevating virus are essential for viral infectivity. J. Virol. 69:613-617.
    • (1995) J. Virol. , vol.69 , pp. 613-617
    • Faaberg, K.S.1    Even, C.2    Palmer, G.A.3    Plagemann, P.G.W.4
  • 10
    • 0028843693 scopus 로고
    • The envelope proteins of lactate dehydrogenase-elevating virus and their membrane topography
    • Faaberg, K. S., and P. G. W. Plagemann. 1995. The envelope proteins of lactate dehydrogenase-elevating virus and their membrane topography. Virology 212:512-525.
    • (1995) Virology , vol.212 , pp. 512-525
    • Faaberg, K.S.1    Plagemann, P.G.W.2
  • 11
    • 0000951677 scopus 로고    scopus 로고
    • Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid
    • Geysen, H. M., H. Meloen, and S. J. Barteling. 1998. Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid. Proc. Natl. Acad. Sci. USA 81:3998-4002.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3998-4002
    • Geysen, H.M.1    Meloen, H.2    Barteling, S.J.3
  • 13
    • 0023713255 scopus 로고
    • Formalin inactivation of the lactate dehydrogenase-elevating virus reveals a major neutralizing epitope not recognized during natural infection
    • Harty, J. T., and P. G. W. Plagemann. 1988. Formalin inactivation of the lactate dehydrogenase-elevating virus reveals a major neutralizing epitope not recognized during natural infection. J. Virol. 62:3210-3216.
    • (1988) J. Virol. , vol.62 , pp. 3210-3216
    • Harty, J.T.1    Plagemann, P.G.W.2
  • 14
    • 0027204176 scopus 로고
    • Glycoprotein E1 of hog cholera virus expressed in insect cells protects swine from hog cholera
    • Hulst, M. M., D. F. Westra, G. Wensvoort, and R. J. M. Moormann. 1993. Glycoprotein E1 of hog cholera virus expressed in insect cells protects swine from hog cholera. J. Virol. 67:5435-5442.
    • (1993) J. Virol. , vol.67 , pp. 5435-5442
    • Hulst, M.M.1    Westra, D.F.2    Wensvoort, G.3    Moormann, R.J.M.4
  • 15
    • 0027130980 scopus 로고
    • Enhanced replication of porcine reproductive and respiratory syndrome virus in a homogeneous subpopulation of MA-104 cell line
    • Kim, H. S., J. Kwang, and I. Y. Yoon. 1993. Enhanced replication of porcine reproductive and respiratory syndrome virus in a homogeneous subpopulation of MA-104 cell line. Arch. Virol. 133:477-483.
    • (1993) Arch. Virol. , vol.133 , pp. 477-483
    • Kim, H.S.1    Kwang, J.2    Yoon, I.Y.3
  • 16
    • 0026095935 scopus 로고
    • A nested set of eight RNAs is formed in macrophages infected with lactate dehydrogenase-elevating virus
    • Kuo, L., J. T. Harty, L. Erickson, G. A. Palmer, and P. G. W. Plagemann. 1991. A nested set of eight RNAs is formed in macrophages infected with lactate dehydrogenase-elevating virus. J. Virol. 65:5118-5123.
    • (1991) J. Virol. , vol.65 , pp. 5118-5123
    • Kuo, L.1    Harty, J.T.2    Erickson, L.3    Palmer, G.A.4    Plagemann, P.G.W.5
  • 17
    • 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 (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0026437265 scopus 로고
    • Comparison and fine mapping of both high and low neutralizing monoclonal antibodies against the principal neutralization domain of HIV-1
    • Langedijk, J. P. M., N. K. T. Back, E. Kinney-Thoma, C. Bruck, M. Francotte, J. Goudsmit, and R. H. Meloen. 1992. Comparison and fine mapping of both high and low neutralizing monoclonal antibodies against the principal neutralization domain of HIV-1. Arch. Virol. 126:129-146.
    • (1992) Arch. Virol. , vol.126 , pp. 129-146
    • Langedijk, J.P.M.1    Back, N.K.T.2    Kinney-Thoma, E.3    Bruck, C.4    Francotte, M.5    Goudsmit, J.6    Meloen, R.H.7
  • 19
    • 0027398130 scopus 로고
    • B-cell epitopes of canine parvovirus: Distribution on the primary structure and exposure on the viral surface
    • Langeveld, J. P. M., J. I. Casal, C. Vela, K. Dalsgaard, S. Smale, W. Puijk, and R. H. Meloen. 1993. B-cell epitopes of canine parvovirus: distribution on the primary structure and exposure on the viral surface. J. Virol. 67:765-772.
    • (1993) J. Virol. , vol.67 , pp. 765-772
    • Langeveld, J.P.M.1    Casal, J.I.2    Vela, C.3    Dalsgaard, K.4    Smale, S.5    Puijk, W.6    Meloen, R.H.7
  • 20
    • 14744304517 scopus 로고
    • A new generation of animal cell expression vectors based on the Semliki Forest virus replicon
    • Liljeström, P., and H. Garoff. 1991. A new generation of animal cell expression vectors based on the Semliki Forest virus replicon. Bio/technology 9:1356-1361.
    • (1991) Bio/technology , vol.9 , pp. 1356-1361
    • Liljeström, P.1    Garoff, H.2
  • 21
    • 40649129000 scopus 로고
    • Expression of proteins using Semliki Forest virus vectors
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. A. Smith, J. G. Seidman, and K. Struhl (ed.), Greene Publishing Associates and Wiley Interscience, New York, N.Y.
    • Liljeström, P., and H. Garoff. 1993. Expression of proteins using Semliki Forest virus vectors, p. 16.xx.1-16.xx.00. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. A. Smith, J. G. Seidman, and K. Struhl (ed.), Current protocols in molecular biology, Greene Publishing Associates and Wiley Interscience, New York, N.Y.
    • (1993) Current Protocols in Molecular Biology
    • Liljeström, P.1    Garoff, H.2
  • 22
    • 0030199284 scopus 로고    scopus 로고
    • Intracellular synthesis, processing and transport of proteins encoded by ORFs 5 to 7 of porcine reproductive and respiratory syndrome virus
    • Mardassi, H., B. Massie, and S. Dea. 1996. Intracellular synthesis, processing and transport of proteins encoded by ORFs 5 to 7 of porcine reproductive and respiratory syndrome virus. Virology 221:98-112.
    • (1996) Virology , vol.221 , pp. 98-112
    • Mardassi, H.1    Massie, B.2    Dea, S.3
  • 23
    • 1842301903 scopus 로고    scopus 로고
    • Unpublished results
    • Meulenberg, J. Unpublished results.
    • Meulenberg, J.1
  • 24
    • 0027242413 scopus 로고
    • Subgenomic RNAs of Lelystad virus contain a conserved junction sequence
    • Meulenberg, J. J. M., E. J. de Meijer, and R. J. M. Moormann. 1993. Subgenomic RNAs of Lelystad virus contain a conserved junction sequence. J. Gen. Virol. 74:1697-1701.
    • (1993) J. Gen. Virol. , vol.74 , pp. 1697-1701
    • Meulenberg, J.J.M.1    De Meijer, E.J.2    Moormann, R.J.M.3
  • 28
    • 0028852340 scopus 로고
    • Comparison of the structural protein coding sequences of the VR-2332 and Lelystad virus strains of the PRRS virus
    • Murtaugh, M. P., M. R. Elam, and Kakach. 1995. Comparison of the structural protein coding sequences of the VR-2332 and Lelystad virus strains of the PRRS virus. Arch. Virol. 140:1451-1460.
    • (1995) Arch. Virol. , vol.140 , pp. 1451-1460
    • Murtaugh, M.P.1    Elam, M.R.2    Kakach3
  • 29
    • 0027332360 scopus 로고
    • Differentiation of United states and european isolates of porcine reproductive and respiratory syndrome virus by monoclonal antibodies
    • Nelson, E. A., J. Christopher-Hennings, T. Drew, G. Wensvoort, J. E. Collins, and D. A. Benfield. 1993. Differentiation of United states and european isolates of porcine reproductive and respiratory syndrome virus by monoclonal antibodies. J. Clin. Microbiol. 31:3184-3189.
    • (1993) J. Clin. Microbiol. , vol.31 , pp. 3184-3189
    • Nelson, E.A.1    Christopher-Hennings, J.2    Drew, T.3    Wensvoort, G.4    Collins, J.E.5    Benfield, D.A.6
  • 30
    • 0026493307 scopus 로고
    • Lactate dehydrogenase-elevating virus, equine arteritis virus, and simian hemorrhagic fever virus: A new group of positive-strand RNA viruses
    • Plagemann, P. G. W., V. and Moennig. 1991. Lactate dehydrogenase-elevating virus, equine arteritis virus, and simian hemorrhagic fever virus: a new group of positive-strand RNA viruses. Adv. Virus Res. 41:99-192.
    • (1991) Adv. Virus Res. , vol.41 , pp. 99-192
    • Plagemann, P.G.W.1    Moennig, V.2
  • 33
    • 0022446364 scopus 로고
    • Production of monoclonal antibodies against swine fever virus and their use in laboratory diagnosis
    • Wensvoort, G., C. Terpstra, J. Boonstra, M. Bloemraad, and D. van Zaane. 1986. Production of monoclonal antibodies against swine fever virus and their use in laboratory diagnosis. Vet. Microbiol. 12:101-108.
    • (1986) Vet. Microbiol. , vol.12 , pp. 101-108
    • Wensvoort, G.1    Terpstra, C.2    Boonstra, J.3    Bloemraad, M.4    Van Zaane, D.5
  • 35
    • 0028899064 scopus 로고
    • Analysis of simian hemorrhagic fever virus (SHFV) subgenomic RNAs, junction sequences and 5′ leader
    • Zeng, L., E. K. Godeny, S. L. Methven, and M. A. Brinton. 1995. Analysis of simian hemorrhagic fever virus (SHFV) subgenomic RNAs, junction sequences and 5′ leader. Virology 207:543-548.
    • (1995) Virology , vol.207 , pp. 543-548
    • Zeng, L.1    Godeny, E.K.2    Methven, S.L.3    Brinton, M.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.