메뉴 건너뛰기




Volumn 72, Issue 2, 1998, Pages 1482-1490

A novel P/V/C gene in a new member of the Paramyxoviridae family, which causes lethal infection in humans, horses, and other animals

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS PROTEIN;

EID: 0031931401     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.2.1482-1490.1998     Document Type: Article
Times cited : (106)

References (51)
  • 1
    • 0028006860 scopus 로고
    • Positive selection vectors using the F plasmid ccdB killer gene
    • Bernard, P., P. Gabant, E. M. Bahassi, and M. Couturier. 1994. Positive selection vectors using the F plasmid ccdB killer gene. Gene 148:71-74.
    • (1994) Gene , vol.148 , pp. 71-74
    • Bernard, P.1    Gabant, P.2    Bahassi, E.M.3    Couturier, M.4
  • 2
    • 0024519674 scopus 로고
    • Measles virus editing provides an additional cysteine-rich protein
    • Cattaneo, R., K. Kaelin, K. Baczko, and M. A. Billeter. 1989. Measles virus editing provides an additional cysteine-rich protein. Cell 56:759-764.
    • (1989) Cell , vol.56 , pp. 759-764
    • Cattaneo, R.1    Kaelin, K.2    Baczko, K.3    Billeter, M.A.4
  • 3
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156.
    • (1987) Anal. Biochem. , vol.162 , pp. 156
    • Chomczynski, P.1    Sacchi, N.2
  • 4
    • 0025783770 scopus 로고
    • The Sendai virus P gene expresses both an essential protein and an inhibitor of RNA synthesis by shuffling modules via mRNA editing
    • Curran, J., R. Boeck, and D. Kolakofsky. 1991. The Sendai virus P gene expresses both an essential protein and an inhibitor of RNA synthesis by shuffling modules via mRNA editing. EMBO J. 10:3079-3085.
    • (1991) EMBO J. , vol.10 , pp. 3079-3085
    • Curran, J.1    Boeck, R.2    Kolakofsky, D.3
  • 5
    • 0028065169 scopus 로고
    • An acidic activation-like domain of the Sendai virus P protein is required for RNA synthesis and encapsidation
    • Curran, J., T. Pelet, and D. Kolakofsky. 1994. An acidic activation-like domain of the Sendai virus P protein is required for RNA synthesis and encapsidation. Virology 202:875-884.
    • (1994) Virology , vol.202 , pp. 875-884
    • Curran, J.1    Pelet, T.2    Kolakofsky, D.3
  • 6
    • 0023411042 scopus 로고
    • Identification of an additional Sendai virus nonstructural protein encoded by the P/C gene mRNA
    • Curran, J. A., and D. Kolakofsky. 1987. Identification of an additional Sendai virus nonstructural protein encoded by the P/C gene mRNA. J. Gen. Virol. 68:2515-2519.
    • (1987) J. Gen. Virol. , vol.68 , pp. 2515-2519
    • Curran, J.A.1    Kolakofsky, D.2
  • 7
    • 0031550528 scopus 로고    scopus 로고
    • Normal cellular replication of Sendai virus without the trans-frame, nonstructural V protein
    • Delenda, C., S. Hausmann, D. Garcin, and D. Kolakofsky. 1997. Normal cellular replication of Sendai virus without the trans-frame, nonstructural V protein. Virology 228:55-62.
    • (1997) Virology , vol.228 , pp. 55-62
    • Delenda, C.1    Hausmann, S.2    Garcin, D.3    Kolakofsky, D.4
  • 8
    • 0014064044 scopus 로고
    • A protein sequenator
    • Edman, P., and C. Begg. 1967. A protein sequenator. Eur. J. Biochem. 1:80-91.
    • (1967) Eur. J. Biochem. , vol.1 , pp. 80-91
    • Edman, P.1    Begg, C.2
  • 11
    • 0026608526 scopus 로고
    • RNA editing in the phosphoprotein gene of the human parainfluenza virus type 3
    • Galinski, M. S., R. M. Troy, and A. K. Banerjee. 1992. RNA editing in the phosphoprotein gene of the human parainfluenza virus type 3. Virology 186:543-550.
    • (1992) Virology , vol.186 , pp. 543-550
    • Galinski, M.S.1    Troy, R.M.2    Banerjee, A.K.3
  • 12
    • 0030199610 scopus 로고    scopus 로고
    • Comparison of the deduced matrix and fusion protein sequences of equine morbillivirus with cognate genes of the Paramyxoviridae
    • Gould, A. R. 1996. Comparison of the deduced matrix and fusion protein sequences of equine morbillivirus with cognate genes of the Paramyxoviridae. Virus Res. 43:17-31.
    • (1996) Virus Res. , vol.43 , pp. 17-31
    • Gould, A.R.1
  • 13
    • 0000140656 scopus 로고    scopus 로고
    • Identification of likely natural hosts for equine morbillivirus
    • Halpin, K., P. Young, and H. Field. 1996. Identification of likely natural hosts for equine morbillivirus. Comm. Dis. Intell. 20:476.
    • (1996) Comm. Dis. Intell. , vol.20 , pp. 476
    • Halpin, K.1    Young, P.2    Field, H.3
  • 14
    • 0028803809 scopus 로고
    • 2- and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself
    • 2-and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself. J. Gen. Virol. 76:2863-2867.
    • (1995) J. Gen. Virol. , vol.76 , pp. 2863-2867
    • Harty, R.N.1    Palese, P.2
  • 15
  • 16
    • 0030225936 scopus 로고    scopus 로고
    • The retrospective diagnosis of a second outbreak of equine morbillivirus infection
    • Hooper, P. G., A. R. Gould, G. M. Russell, J. A. Kattenbelt, and G. Mitchell. 1996. The retrospective diagnosis of a second outbreak of equine morbillivirus infection. Aust. Vet. J. 74:244-245.
    • (1996) Aust. Vet. J. , vol.74 , pp. 244-245
    • Hooper, P.G.1    Gould, A.R.2    Russell, G.M.3    Kattenbelt, J.A.4    Mitchell, G.5
  • 17
    • 0030200354 scopus 로고    scopus 로고
    • Ultrastructure of equine morbillivirus
    • Hyatt, A. D., and P. W. Selleck. 1996. Ultrastructure of equine morbillivirus. Virus Res. 43:1-15.
    • (1996) Virus Res. , vol.43 , pp. 1-15
    • Hyatt, A.D.1    Selleck, P.W.2
  • 18
    • 0031022055 scopus 로고    scopus 로고
    • The paramyxovirus, Sendai virus, V protein encodes a luxury function required for viral pathogenesis
    • Kato, A., K. Kiyotani, Y. Sakai, T. Yoshida, and Y. Nagai. 1997. The paramyxovirus, Sendai virus, V protein encodes a luxury function required for viral pathogenesis. EMBO J. 16:578-587.
    • (1997) EMBO J. , vol.16 , pp. 578-587
    • Kato, A.1    Kiyotani, K.2    Sakai, Y.3    Yoshida, T.4    Nagai, Y.5
  • 19
    • 0030852445 scopus 로고    scopus 로고
    • Importance of the cysteine-rich carboxyl-terminal half of V protein for Sendai virus pathogenesis
    • Kato, A., K. Kiyotani, Y. Sakai, T. Yoshida, T. Shioda, and Y. Nagai. 1997. Importance of the cysteine-rich carboxyl-terminal half of V protein for Sendai virus pathogenesis. J. Virol. 71:7266-7272.
    • (1997) J. Virol. , vol.71 , pp. 7266-7272
    • Kato, A.1    Kiyotani, K.2    Sakai, Y.3    Yoshida, T.4    Shioda, T.5    Nagai, Y.6
  • 20
    • 0025792297 scopus 로고
    • Structural features in eukaryotic mRNAs that modulate the initiation of translation
    • Kozak, M. 1991. Structural features in eukaryotic mRNAs that modulate the initiation of translation. J. Biol. Chem. 266:19867-19870.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19867-19870
    • Kozak, M.1
  • 21
    • 0029971736 scopus 로고    scopus 로고
    • Normal replication of vesicular stomatitis virus without C proteins
    • Kretzschmar, E., R. Peluso, M. J. Schnell, M. A. Whitt, and J. K. Rose. 1996. Normal replication of vesicular stomatitis virus without C proteins. Virology 216:309-316.
    • (1996) Virology , vol.216 , pp. 309-316
    • Kretzschmar, E.1    Peluso, R.2    Schnell, M.J.3    Whitt, M.A.4    Rose, J.K.5
  • 22
    • 0028181441 scopus 로고
    • Hidden Markov models in computational biology: Applications to protein modeling
    • Krogh, A., M. Brown, I. S. Mian, K. Sjolander, and D. Haussler. 1994. Hidden Markov models in computational biology: applications to protein modeling. J. Mol. Biol. 235:1501-1531.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1501-1531
    • Krogh, A.1    Brown, M.2    Mian, I.S.3    Sjolander, K.4    Haussler, D.5
  • 23
    • 0001178028 scopus 로고    scopus 로고
    • Paramyxoviridae: The viruses and their replication
    • B. N. Fields et al. (ed.), Lippincott-Raven Publishers, Philadelphia, Pa.
    • Lamb, R. A., and D. Kolakofsky. 1996. Paramyxoviridae: the viruses and their replication, p. 1177-1204. In B. N. Fields et al. (ed.), Fields virology, 3rd ed. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 1177-1204
    • Lamb, R.A.1    Kolakofsky, D.2
  • 24
    • 0028339165 scopus 로고
    • Measles virus V protein binds zinc
    • Liston, P., and D. J. Briedis. 1994. Measles virus V protein binds zinc. Virology 198:399-404.
    • (1994) Virology , vol.198 , pp. 399-404
    • Liston, P.1    Briedis, D.J.2
  • 25
    • 0028846589 scopus 로고
    • Protein interactions entered into by the measles virus P, V, and C proteins
    • Liston, P., C. Di Flumeri, and D. J. Briedis. 1995. Protein interactions entered into by the measles virus P, V, and C proteins. Virus Res. 38:241-259.
    • (1995) Virus Res. , vol.38 , pp. 241-259
    • Liston, P.1    Di Flumeri, C.2    Briedis, D.J.3
  • 26
    • 0026092057 scopus 로고
    • The P gene of human parainfluenza virus type 1 encodes P and C proteins but not a cysteine-rich V protein
    • Matsuoka, Y., J. Curran, T. Pelet, D. Kolakofsky, R. Ray, and R. W. Compans. 1991. The P gene of human parainfluenza virus type 1 encodes P and C proteins but not a cysteine-rich V protein. J. Virol. 65:3406-3410.
    • (1991) J. Virol. , vol.65 , pp. 3406-3410
    • Matsuoka, Y.1    Curran, J.2    Pelet, T.3    Kolakofsky, D.4    Ray, R.5    Compans, R.W.6
  • 27
    • 0018842968 scopus 로고
    • A comparison of the structural polypeptides of five strains of mumps virus
    • McCarthy, M., and R. T. Johnson. 1980. A comparison of the structural polypeptides of five strains of mumps virus. J. Gen. Virol. 46:15-27.
    • (1980) J. Gen. Virol. , vol.46 , pp. 15-27
    • McCarthy, M.1    Johnson, R.T.2
  • 28
    • 77957091724 scopus 로고
    • Rapid separation of proteins and peptides using conventional silica-based supports: Identification of 2-D gel proteins following in-gel proteolysis
    • J. W. Crabb (ed.), Academic Press, New York, N.Y.
    • Moritz, R. L., J. Eddes, H. Ji, G. E. Reid, and R. J. Simpson. 1995. Rapid separation of proteins and peptides using conventional silica-based supports: identification of 2-D gel proteins following in-gel proteolysis, p. 311-319. In J. W. Crabb (ed.), Techniques in protein chemistry, vol. VI. Academic Press, New York, N.Y.
    • (1995) Techniques in Protein Chemistry , vol.6 , pp. 311-319
    • Moritz, R.L.1    Eddes, J.2    Ji, H.3    Reid, G.E.4    Simpson, R.J.5
  • 30
    • 0002641210 scopus 로고    scopus 로고
    • Flying foxes, horses, and humans: A zoonosis caused by a new member of the Paramyxoviridae
    • W. M. Scheld, D. Armstrong, and J. M. Hughes (ed.), ASM Press, Washington, D.C.
    • Murray, P. K., B. T. Eaton, P. Hooper, L. Wang, M. Williamson, and P. Young. 1998. Flying foxes, horses, and humans: a zoonosis caused by a new member of the Paramyxoviridae, p. 43-58. In W. M. Scheld, D. Armstrong, and J. M. Hughes (ed.), Emerging infections. ASM Press, Washington, D.C.
    • (1998) Emerging Infections , pp. 43-58
    • Murray, P.K.1    Eaton, B.T.2    Hooper, P.3    Wang, L.4    Williamson, M.5    Young, P.6
  • 32
    • 0028964081 scopus 로고
    • The paramyxovirus SV5 V protein binds two atoms of zinc and is a structural component of virions
    • Paterson, R. G., G. P. Leser, M. A. Shaughnessy, and R. A. Lamb. 1995. The paramyxovirus SV5 V protein binds two atoms of zinc and is a structural component of virions. Virology 208:121-131.
    • (1995) Virology , vol.208 , pp. 121-131
    • Paterson, R.G.1    Leser, G.P.2    Shaughnessy, M.A.3    Lamb, R.A.4
  • 33
    • 0026068757 scopus 로고
    • The P gene of bovine parainfluenza virus 3 expresses all three reading frames from a single mRNA editing site
    • Pelet, T., J. Curran, and D. Kolakofsky. 1991. The P gene of bovine parainfluenza virus 3 expresses all three reading frames from a single mRNA editing site. EMBO J. 10:443-448.
    • (1991) EMBO J. , vol.10 , pp. 443-448
    • Pelet, T.1    Curran, J.2    Kolakofsky, D.3
  • 34
    • 0026703670 scopus 로고
    • Loss of V protein expression in human parainfluenza virus type 1 is not a recent event
    • Rochat, S., H. Komada, and D. Kolakofsky. 1992. Loss of V protein expression in human parainfluenza virus type 1 is not a recent event. Virus Res. 24:137-144.
    • (1992) Virus Res. , vol.24 , pp. 137-144
    • Rochat, S.1    Komada, H.2    Kolakofsky, D.3
  • 36
    • 0026004135 scopus 로고
    • Two noncontiguous regions of the Sendai virus P protein combine to form a single nucleocapsid binding site
    • Ryan, K. W., E. M. Morgan, and A. Portner. 1991. Two noncontiguous regions of the Sendai virus P protein combine to form a single nucleocapsid binding site. Virology 180:126-134.
    • (1991) Virology , vol.180 , pp. 126-134
    • Ryan, K.W.1    Morgan, E.M.2    Portner, A.3
  • 37
    • 0031579250 scopus 로고    scopus 로고
    • Recombinant measles viruses defective for RNA editing and V protein synthesis are viable in cultured cells
    • Schneider, H., K. Kaelin, and M. A. Billeter. 1997. Recombinant measles viruses defective for RNA editing and V protein synthesis are viable in cultured cells. Virology 227:314-322.
    • (1997) Virology , vol.227 , pp. 314-322
    • Schneider, H.1    Kaelin, K.2    Billeter, M.A.3
  • 40
    • 0027273314 scopus 로고
    • A small highly basic protein is encoded in overlapping frame within the P gene of vesicular stomatitis virus
    • Spiropoulou, C. F., and S. T. Nichol. 1993. A small highly basic protein is encoded in overlapping frame within the P gene of vesicular stomatitis virus. J. Virol. 67:3103-3110.
    • (1993) J. Virol. , vol.67 , pp. 3103-3110
    • Spiropoulou, C.F.1    Nichol, S.T.2
  • 41
    • 0018410960 scopus 로고
    • Purification of measles virus and characterization of subviral components
    • Stallcup, K. C., S. L. Wechsler, and B. N. Fields. 1979. Purification of measles virus and characterization of subviral components. J. Virol. 30:166-176.
    • (1979) J. Virol. , vol.30 , pp. 166-176
    • Stallcup, K.C.1    Wechsler, S.L.2    Fields, B.N.3
  • 42
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. 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.J.3
  • 43
    • 0023896254 scopus 로고
    • Mapping of monoclonal antibodies to the Sendai virus P protein and the location of its phosphates
    • Vidal, S., J. Curran, C. Orvell, and D. Kolakofsky. 1988. Mapping of monoclonal antibodies to the Sendai virus P protein and the location of its phosphates. J. Virol. 62:2200-2203.
    • (1988) J. Virol. , vol.62 , pp. 2200-2203
    • Vidal, S.1    Curran, J.2    Orvell, C.3    Kolakofsky, D.4
  • 44
    • 0025141746 scopus 로고
    • Editing of the Sendai virus P/C mRNA by G insertion occurs during mRNA synthesis via a virus-encoded activity
    • Vidal, S., J. Curran, and D. Kolakofsky. 1990. Editing of the Sendai virus P/C mRNA by G insertion occurs during mRNA synthesis via a virus-encoded activity. J. Virol. 64:239-246.
    • (1990) J. Virol. , vol.64 , pp. 239-246
    • Vidal, S.1    Curran, J.2    Kolakofsky, D.3
  • 45
    • 0028801675 scopus 로고
    • Use of a gene-targeted phage display random epitope library to map an antigenic determinant on the bluetongue virus outer capsid protein VP5
    • Wang, L.-F., D. H. Du Plessis, J. R. White, A. D. Hyatt, and B. T. Eaton. 1995. Use of a gene-targeted phage display random epitope library to map an antigenic determinant on the bluetongue virus outer capsid protein VP5. J. Immunol. Methods 178:1-12.
    • (1995) J. Immunol. Methods , vol.178 , pp. 1-12
    • Wang, L.-F.1    Du Plessis, D.H.2    White, J.R.3    Hyatt, A.D.4    Eaton, B.T.5
  • 47
    • 0030003654 scopus 로고    scopus 로고
    • BTag: A novel six-residue epitope tag for surveillance and purification of recombinant proteins
    • Wang, L.-F., M. Yu, J. R. White, and B. T. Eaton. 1996. BTag: a novel six-residue epitope tag for surveillance and purification of recombinant proteins. Gene 169:53-58.
    • (1996) Gene , vol.169 , pp. 53-58
    • Wang, L.-F.1    Yu, M.2    White, J.R.3    Eaton, B.T.4
  • 48
    • 0022341707 scopus 로고
    • Human parainfluenza virus 3: Purification and characterization of subviral components and viral RNA
    • Wechsler, S. L., D. M. Lambert, M. S. Galinski, B. E. Heineke, and M. W. Pons. 1985. Human parainfluenza virus 3: purification and characterization of subviral components and viral RNA. Virus Res. 3:339-351.
    • (1985) Virus Res. , vol.3 , pp. 339-351
    • Wechsler, S.L.1    Lambert, D.M.2    Galinski, M.S.3    Heineke, B.E.4    Pons, M.W.5
  • 49
    • 0029331121 scopus 로고
    • Equine morbillivirus pneumonia: Susceptibility of laboratory animals to the virus
    • Westbury, H. A., P. T. Hooper, P. W. Selleck, and P. K. Murray. 1995. Equine morbillivirus pneumonia: susceptibility of laboratory animals to the virus. Aust. Vet. J. 72:278-279.
    • (1995) Aust. Vet. J. , vol.72 , pp. 278-279
    • Westbury, H.A.1    Hooper, P.T.2    Selleck, P.W.3    Murray, P.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.