메뉴 건너뛰기




Volumn 91, Issue 2, 2003, Pages 181-187

Differential stability and fusion activity of Lyssavirus glycoprotein trimers

Author keywords

Fusion; Glycoprotein; Lyssavirus; Mokola; Rabies; Trimer

Indexed keywords

3 [(3 CHOLAMIDOPROPYL)DIMETHYLAMMONIO] 1 PROPANESULFONIC ACID; GLYCOPROTEIN; SUCROSE; VIRUS PROTEIN;

EID: 0037308452     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1702(02)00267-8     Document Type: Article
Times cited : (25)

References (37)
  • 1
    • 0035100866 scopus 로고    scopus 로고
    • Evidence of two Lyssavirus phylogroups with distinct pathogenicity
    • Badrane H., Bahloul C., Perrin P., Tordo N. Evidence of two Lyssavirus phylogroups with distinct pathogenicity. J. Virol. 75:2001;3268-3276.
    • (2001) J. Virol. , vol.75 , pp. 3268-3276
    • Badrane, H.1    Bahloul, C.2    Perrin, P.3    Tordo, N.4
  • 2
    • 0032007830 scopus 로고    scopus 로고
    • DNA-based immunization for exploring the enlargement of immunological cross-reactivity against the Lyssaviruses
    • Bahloul C., Jacob Y., Tordo N., Perrin P. DNA-based immunization for exploring the enlargement of immunological cross-reactivity against the Lyssaviruses. Vaccine. 6:1998;417-425.
    • (1998) Vaccine , vol.6 , pp. 417-425
    • Bahloul, C.1    Jacob, Y.2    Tordo, N.3    Perrin, P.4
  • 3
    • 0027237788 scopus 로고
    • Molecular diversity of the Lyssavirus genus
    • Bourhy H., Kissi B., Tordo N. Molecular diversity of the Lyssavirus genus. Virology. 194:1993;70-81.
    • (1993) Virology , vol.194 , pp. 70-81
    • Bourhy, H.1    Kissi, B.2    Tordo, N.3
  • 4
    • 0019833603 scopus 로고
    • Structure of the rabies virus: Spatial relationships of the proteins G, M1, M2 and N
    • Delagneau J.-F., Perrin P., Atanasiu P. Structure of the rabies virus: spatial relationships of the proteins G, M1, M2 and N. Ann. Virol. (Inst. Pasteur). 132:1981;473-493.
    • (1981) Ann. Virol. (Inst. Pasteur) , vol.132 , pp. 473-493
    • Delagneau, J.-F.1    Perrin, P.2    Atanasiu, P.3
  • 5
    • 0017686060 scopus 로고
    • Oligosaccharides of the glycoprotein of rabies virus
    • Dietzschold B. Oligosaccharides of the glycoprotein of rabies virus. J. Virol. 23:1977;286-293.
    • (1977) J. Virol. , vol.23 , pp. 286-293
    • Dietzschold, B.1
  • 6
    • 0023550869 scopus 로고
    • Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers
    • Doms R.W., Keller D.S., Helenius A., Balch W.E. Role for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers. J. Cell Biol. 105:1987;1957-1969.
    • (1987) J. Cell Biol. , vol.105 , pp. 1957-1969
    • Doms, R.W.1    Keller, D.S.2    Helenius, A.3    Balch, W.E.4
  • 8
    • 0024212083 scopus 로고
    • Efficacy of rabies vaccines against Duvenhage virus isolated from European house bats (Eptesicus serotinus), classic rabies and rabies-related viruses
    • Fekadu M., Shaddock J., Sanderlin D., Smith J. Efficacy of rabies vaccines against Duvenhage virus isolated from European house bats (Eptesicus serotinus), classic rabies and rabies-related viruses. Vaccine. 6:1988;533-539.
    • (1988) Vaccine , vol.6 , pp. 533-539
    • Fekadu, M.1    Shaddock, J.2    Sanderlin, D.3    Smith, J.4
  • 10
    • 0026018237 scopus 로고
    • Reversible conformational changes and fusion activity of rabies virus glycoprotein
    • Gaudin Y., Tuffereau C., Segretain D., Knossow M., Flamand A. Reversible conformational changes and fusion activity of rabies virus glycoprotein. J. Virol. 65:1991;4853-4859.
    • (1991) J. Virol. , vol.65 , pp. 4853-4859
    • Gaudin, Y.1    Tuffereau, C.2    Segretain, D.3    Knossow, M.4    Flamand, A.5
  • 12
    • 0029795034 scopus 로고    scopus 로고
    • Identification of amino acids controlling the low-pH-induced conformational change of rabies virus glycoprotein
    • Gaudin Y., Raux H., Flamand A., Ruigrok R. Identification of amino acids controlling the low-pH-induced conformational change of rabies virus glycoprotein. J. Virol. 70:1996;7371-7378.
    • (1996) J. Virol. , vol.70 , pp. 7371-7378
    • Gaudin, Y.1    Raux, H.2    Flamand, A.3    Ruigrok, R.4
  • 13
    • 0032986746 scopus 로고    scopus 로고
    • Soluble ectodomain of rabies virus glycoprotein expressed in eukaryotic cells folds in a monomeric conformation that is antigenically distinct from the native state of the complete, membrane-anchored glycoprotein
    • Gaudin Y., Moreira S., Bénéjean J., Blondel D., Flamand A., Tuffereau C. Soluble ectodomain of rabies virus glycoprotein expressed in eukaryotic cells folds in a monomeric conformation that is antigenically distinct from the native state of the complete, membrane-anchored glycoprotein. J. Gen. Virol. 80:1999;1647-1656.
    • (1999) J. Gen. Virol. , vol.80 , pp. 1647-1656
    • Gaudin, Y.1    Moreira, S.2    Bénéjean, J.3    Blondel, D.4    Flamand, A.5    Tuffereau, C.6
  • 16
    • 0002744579 scopus 로고
    • Rabies-related viruses
    • J.B. Campbell, & K.M. Charlton. Boston: Kluwer
    • King A., Crick J. Rabies-related viruses. Campbell J.B., Charlton K.M. Rabies. 1988;117-199 Kluwer, Boston.
    • (1988) Rabies , pp. 117-199
    • King, A.1    Crick, J.2
  • 17
    • 0022857630 scopus 로고
    • Binding of rabies virus to purified torpedo acetylcholine receptor
    • Lentz T., Benson R., Klimowicz D., Wilson P. Binding of rabies virus to purified torpedo acetylcholine receptor. Mol. Brain Res. 1:1986;211-219.
    • (1986) Mol. Brain Res. , vol.1 , pp. 211-219
    • Lentz, T.1    Benson, R.2    Klimowicz, D.3    Wilson, P.4
  • 18
    • 0036271962 scopus 로고    scopus 로고
    • Rabies virus glycoprotein can fold in two alternative antigenically distinct conformations depending on membrane anchor type
    • Maillard A.P., Gaudin Y. Rabies virus glycoprotein can fold in two alternative antigenically distinct conformations depending on membrane anchor type. J. Gen. Virol. 83:2002;1465-1476.
    • (2002) J. Gen. Virol. , vol.83 , pp. 1465-1476
    • Maillard, A.P.1    Gaudin, Y.2
  • 19
    • 0028801967 scopus 로고
    • Mokola virus glycoprotein and chimeric proteins can replace rabies virus glycoprotein in the rescue of infectious defective rabies virus particles
    • Mebatsion T., Schnell M.J., Conzelmann K.K. Mokola virus glycoprotein and chimeric proteins can replace rabies virus glycoprotein in the rescue of infectious defective rabies virus particles. J. Virol. 69:1995;1444-1451.
    • (1995) J. Virol. , vol.69 , pp. 1444-1451
    • Mebatsion, T.1    Schnell, M.J.2    Conzelmann, K.K.3
  • 20
    • 17344368263 scopus 로고    scopus 로고
    • Pathogenicity of different rabies variants inversely correlates with apoptosis and rabies virus glycoprotein expression in infected primary neuron culture
    • Morimoto K., Hooper C., Spitsin S., Koprowski H., Dietzschold B. Pathogenicity of different rabies variants inversely correlates with apoptosis and rabies virus glycoprotein expression in infected primary neuron culture. J. Virol. 73:1999;510-518.
    • (1999) J. Virol. , vol.73 , pp. 510-518
    • Morimoto, K.1    Hooper, C.2    Spitsin, S.3    Koprowski, H.4    Dietzschold, B.5
  • 21
    • 0018763470 scopus 로고
    • Regulation of simian virus 40 transcription: Sensitive analysis of the RNA species present early in infections by virus DNA
    • Parker B., Stark G. Regulation of simian virus 40 transcription: sensitive analysis of the RNA species present early in infections by virus DNA. J. Virol. 31:1979;360-369.
    • (1979) J. Virol. , vol.31 , pp. 360-369
    • Parker, B.1    Stark, G.2
  • 22
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signaling from the endoplasmic reticulum to the nucleus: The unfolded protein response in yeast and mammals
    • Patil C., Walter P. Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr. Opin. Cell Biol. 13:2001;349-355.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 349-355
    • Patil, C.1    Walter, P.2
  • 23
    • 0001872910 scopus 로고    scopus 로고
    • Techniques for the preparation of rabies conjugates
    • F.-X. Meslin, M. Kaplan, & H. Koprowski. Geneva: WHO
    • Perrin P. Techniques for the preparation of rabies conjugates. Meslin F.-X., Kaplan M., Koprowski H. Laboratory Techniques in Rabies. fourth ed. 1996;433-445 WHO, Geneva.
    • (1996) Laboratory Techniques in Rabies fourth ed. , pp. 433-445
    • Perrin, P.1
  • 24
    • 0018872260 scopus 로고
    • Partial structural study of oligosides of rabies virus glycoprotein
    • Perrin P., Atanasiu P. Partial structural study of oligosides of rabies virus glycoprotein. Microbiology. 3:1980;57-74.
    • (1980) Microbiology , vol.3 , pp. 57-74
    • Perrin, P.1    Atanasiu, P.2
  • 25
    • 0022415294 scopus 로고
    • Rabies immunosomes (subunit vaccine) structure and immunogenicity. Pre- and post-exposure protection studies
    • Perrin P., Thibodeau L., Sureau P. Rabies immunosomes (subunit vaccine) structure and immunogenicity. Pre- and post-exposure protection studies. Vaccine. 3:1985;325-332.
    • (1985) Vaccine , vol.3 , pp. 325-332
    • Perrin, P.1    Thibodeau, L.2    Sureau, P.3
  • 26
    • 0022549583 scopus 로고
    • A rapid rabies enzyme immuno-diagnosis (RREID): A useful and simple technique for the routine diagnosis of rabies
    • Perrin P., Rollin P., Sureau P. A rapid rabies enzyme immuno-diagnosis (RREID): a useful and simple technique for the routine diagnosis of rabies. J. Biol. Standard. 14:1986;217-222.
    • (1986) J. Biol. Standard , vol.14 , pp. 217-222
    • Perrin, P.1    Rollin, P.2    Sureau, P.3
  • 27
    • 0023750140 scopus 로고
    • Interleukin-2 production in vitro: A new approach to the study of rabies vaccine immunogenicity as appraised by testing different glycoprotein presentations
    • Perrin P., Joffret M.-L., Oth D., Leclerc C., Sureau P., Thibodeau L. Interleukin-2 production in vitro: a new approach to the study of rabies vaccine immunogenicity as appraised by testing different glycoprotein presentations. Vaccine. 6:1988;331-338.
    • (1988) Vaccine , vol.6 , pp. 331-338
    • Perrin, P.1    Joffret, M.-L.2    Oth, D.3    Leclerc, C.4    Sureau, P.5    Thibodeau, L.6
  • 28
    • 0030248622 scopus 로고    scopus 로고
    • The antigen-specific cell-mediated immune response in mice is suppressed by infection with pathogenic lyssaviruses
    • Perrin P., De Franco M., Jallet C., Fouque F., Morgeaux S., Tordo N., Colle J.-H. The antigen-specific cell-mediated immune response in mice is suppressed by infection with pathogenic lyssaviruses. Res. Virol. 147:1996;289-299.
    • (1996) Res. Virol. , vol.147 , pp. 289-299
    • Perrin, P.1    De Franco, M.2    Jallet, C.3    Fouque, F.4    Morgeaux, S.5    Tordo, N.6    Colle, J.-H.7
  • 29
    • 0017342307 scopus 로고
    • Plaque formation of herpes virus hominis type 2 and rubella virus in variants isolated from the colonies of BHK-21/WI-2 cells formed in soft agar
    • Sato M., Maeda N., Yoshida H., Urade M., Saito S., Miyazaki T., Shibata T., Watanabe M. Plaque formation of herpes virus hominis type 2 and rubella virus in variants isolated from the colonies of BHK-21/WI-2 cells formed in soft agar. Arch. Virol. 53:1977;269-273.
    • (1977) Arch. Virol. , vol.53 , pp. 269-273
    • Sato, M.1    Maeda, N.2    Yoshida, H.3    Urade, M.4    Saito, S.5    Miyazaki, T.6    Shibata, T.7    Watanabe, M.8
  • 31
    • 0032535485 scopus 로고    scopus 로고
    • Low-affinity nerve-growth factor receptor (P75NTR) can serve as a receptor for rabies virus
    • Tuffereau C., Bénéjean J., Blondel D., Kieffer B., Flamand A. Low-affinity nerve-growth factor receptor (P75NTR) can serve as a receptor for rabies virus. EMBO J. 17:1998;7250-7259.
    • (1998) EMBO J. , vol.17 , pp. 7250-7259
    • Tuffereau, C.1    Bénéjean, J.2    Blondel, D.3    Kieffer, B.4    Flamand, A.5
  • 33
    • 0026339191 scopus 로고
    • Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein
    • Whitt M., Buonocore L., Prehaud C., Rose J. Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein. Virology. 185:1991;681-688.
    • (1991) Virology , vol.185 , pp. 681-688
    • Whitt, M.1    Buonocore, L.2    Prehaud, C.3    Rose, J.4
  • 35
    • 0028931761 scopus 로고
    • Stable secretion of a soluble oligomeric form of rabies virus glycoprotein: Influence of N-glycan processing on secretion
    • Wojczyk B., Shakin-Eshleman S., Doms R., Xiang Z., Ertl H., Wunner W., Spitalnik S. Stable secretion of a soluble oligomeric form of rabies virus glycoprotein: influence of N-glycan processing on secretion. Biochemistry. 34:1995;2599-2609.
    • (1995) Biochemistry , vol.34 , pp. 2599-2609
    • Wojczyk, B.1    Shakin-Eshleman, S.2    Doms, R.3    Xiang, Z.4    Ertl, H.5    Wunner, W.6    Spitalnik, S.7
  • 36
    • 0036689346 scopus 로고    scopus 로고
    • The rabies virus glycoprotein determines the distribution of different rabies virus strains in the brain
    • Yan X., Mohankumar P.S., Dietzschold B., Schnell M.J., Fu Z.F. The rabies virus glycoprotein determines the distribution of different rabies virus strains in the brain. J. Neurovirol. 8:2002;345-352.
    • (2002) J. Neurovirol. , vol.8 , pp. 345-352
    • Yan, X.1    Mohankumar, P.S.2    Dietzschold, B.3    Schnell, M.J.4    Fu, Z.F.5
  • 37
    • 0031202401 scopus 로고    scopus 로고
    • Protective antibody responses against viruses
    • Zinkernagel R. Protective antibody responses against viruses. Biol. Chem. 378:1997;725-729.
    • (1997) Biol. Chem. , vol.378 , pp. 725-729
    • Zinkernagel, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.