메뉴 건너뛰기




Volumn 70, Issue 4, 1996, Pages 2237-2246

Calnexin acts as a molecular chaperone during the folding of glycoprotein B of human cytomegalovirus

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CASTANOSPERMINE; CHAPERONE; TUNICAMYCIN; VIRUS GLYCOPROTEIN;

EID: 0029872240     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.70.4.2237-2246.1996     Document Type: Article
Times cited : (31)

References (53)
  • 1
    • 1842268100 scopus 로고
    • Cytomegalovirus
    • B N. Fields (ed), Raven Press, New York
    • Alford, C.A., Jr., and W.J. Britt. 1985 Cytomegalovirus, p-629-660. In B N. Fields (ed), Virology Raven Press, New York
    • (1985) Virology , pp. 629-660
    • Alford Jr., C.A.1    Britt, W.J.2
  • 2
    • 0028946717 scopus 로고
    • Intracellular folding of tissue-type plasminogen activator
    • Allen, S., H. Y. Naim, and N. J. Bulleid. 1995. Intracellular folding of tissue-type plasminogen activator. J Biol. Chem 270:4797-4804.
    • (1995) J Biol. Chem , vol.270 , pp. 4797-4804
    • Allen, S.1    Naim, H.Y.2    Bulleid, N.J.3
  • 3
    • 0028152358 scopus 로고
    • A role for calnexin (IP90) in the assembly of class II MHC molecules
    • Anderson, K. S., and P. Cresswell. 1994. A role for calnexin (IP90) in the assembly of class II MHC molecules. EMBO J. 13:675-682.
    • (1994) EMBO J. , vol.13 , pp. 675-682
    • Anderson, K.S.1    Cresswell, P.2
  • 4
    • 0022529476 scopus 로고
    • Primate cytomegalovirus glycoproteins: Lectin-binding properties and sensitivities to glycosidases
    • Benko, D. M., and W. Gibson. 1986. Primate cytomegalovirus glycoproteins: lectin-binding properties and sensitivities to glycosidases. J. Virol. 59:703-713
    • (1986) J. Virol. , vol.59 , pp. 703-713
    • Benko, D.M.1    Gibson, W.2
  • 6
    • 0026508087 scopus 로고
    • Role of ATP and disulfide bonds during protein folding in the endoplasmic reticulum
    • Braakman, I., J. Helenius, and A. Helenius. 1992. Role of ATP and disulfide bonds during protein folding in the endoplasmic reticulum. Nature (London) 356:260-262
    • (1992) Nature (London) , vol.356 , pp. 260-262
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 7
    • 0026604334 scopus 로고
    • Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum
    • Braakman, I., J. Helenins, and A. Helenius. 1992. Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. EMBO J. 11:1717-1722.
    • (1992) EMBO J. , vol.11 , pp. 1717-1722
    • Braakman, I.1    Helenins, J.2    Helenius, A.3
  • 8
    • 0025816663 scopus 로고
    • Folding of influenza hemagglutinin in the endoplasmic reticulum
    • Braakman, I., H. Hoover-Litty, K. R. Wagner, and A. Helenius. 1991. Folding of influenza hemagglutinin in the endoplasmic reticulum. J. Cell Biol. 114:401-411.
    • (1991) J. Cell Biol. , vol.114 , pp. 401-411
    • Braakman, I.1    Hoover-Litty, H.2    Wagner, K.R.3    Helenius, A.4
  • 9
    • 0025738528 scopus 로고
    • Recent advances in the identification of significant human cytomegalovirus-encoded proteins
    • Britt, W. J. 1991. Recent advances in the identification of significant human cytomegalovirus-encoded proteins Transplant. Proc 23:64-69.
    • (1991) Transplant. Proc , vol.23 , pp. 64-69
    • Britt, W.J.1
  • 10
    • 0022470497 scopus 로고
    • Synthesis and processing of the envelope gp55-116 complex of human cytomegalovirus
    • Britt, W. J., and D. Auger. 1986. Synthesis and processing of the envelope gp55-116 complex of human cytomegalovirus. J. Virol 58:185-191.
    • (1986) J. Virol , vol.58 , pp. 185-191
    • Britt, W.J.1    Auger, D.2
  • 11
    • 0024585227 scopus 로고
    • Processing of the gp55-116 envelope glycoprotein complex (gB) of human cytomegalovirus
    • Britt, W. J., and L. Vulger. 1989. Processing of the gp55-116 envelope glycoprotein complex (gB) of human cytomegalovirus. J. Virol. 63:403-110.
    • (1989) J. Virol. , vol.63 , pp. 403-1110
    • Britt, W.J.1    Vulger, L.2
  • 12
    • 0021402758 scopus 로고
    • Inhibition of N-linked oligosaccharide trimming does not interfere with surface expression of certain integral membrane proteins
    • Burke, B., K. Matlin, E. Bause, G. Legler, N. Peyrieras, and H. Ploegh. 1984. Inhibition of N-linked oligosaccharide trimming does not interfere with surface expression of certain integral membrane proteins. EMBO J. 3:551-556.
    • (1984) EMBO J. , vol.3 , pp. 551-556
    • Burke, B.1    Matlin, K.2    Bause, E.3    Legler, G.4    Peyrieras, N.5    Ploegh, H.6
  • 14
    • 0022555899 scopus 로고
    • Disulfide bonds as probes of protein folding pathways
    • Creighton, T. E. 1986. Disulfide bonds as probes of protein folding pathways. Methods Enzymol. 131:83-106.
    • (1986) Methods Enzymol. , vol.131 , pp. 83-106
    • Creighton, T.E.1
  • 15
    • 0027156495 scopus 로고
    • Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin)
    • David, V., F. Hochstenbach, S. Rajagopalan, and M. Brenner. 1993. Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin) J Biol. Chem. 268:9585-9592.
    • (1993) J Biol. Chem. , vol.268 , pp. 9585-9592
    • David, V.1    Hochstenbach, F.2    Rajagopalan, S.3    Brenner, M.4
  • 16
    • 0026528005 scopus 로고
    • Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both β2-microglobulin and peptide
    • Degen, E., M. F. Cohen-Doyle, and D. B. Williams. 1992. Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both β2-microglobulin and peptide. J. Exp. Med 175:1653-1661.
    • (1992) J. Exp. Med , vol.175 , pp. 1653-1661
    • Degen, E.1    Cohen-Doyle, M.F.2    Williams, D.B.3
  • 17
    • 0026022577 scopus 로고
    • Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules
    • Degen, E., and D. B. Williams. 1991. Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules. J Cell Biol. 112:1099-1115.
    • (1991) J Cell Biol. , vol.112 , pp. 1099-1115
    • Degen, E.1    Williams, D.B.2
  • 18
    • 0023159808 scopus 로고
    • Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains
    • Elbein, A. D. 1987. Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains. Annu. Rev. Biochem. 56:497-534.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 497-534
    • Elbein, A.D.1
  • 19
    • 0026317511 scopus 로고
    • Glycosidase inhibitors: Inhibitors of N-linked oligosaccharide processing
    • Elbein, A. D. 1991. Glycosidase inhibitors: inhibitors of N-linked oligosaccharide processing. FASEB J. 5:3055-3063.
    • (1991) FASEB J. , vol.5 , pp. 3055-3063
    • Elbein, A.D.1
  • 20
    • 0022844021 scopus 로고
    • Prospects for the clinical management of human cytomegalovirus infections
    • Farrar, G. H., J. R. Bull, and P. J. Greenaway. 1986. Prospects for the clinical management of human cytomegalovirus infections. Vaccine 4:217-224.
    • (1986) Vaccine , vol.4 , pp. 217-224
    • Farrar, G.H.1    Bull, J.R.2    Greenaway, P.J.3
  • 21
    • 0000870776 scopus 로고
    • Native disulfide bond formation in protein biosynthesis evidence for the role of protein disulfide isomerase
    • Freedman, R. B. 1984. Native disulfide bond formation in protein biosynthesis evidence for the role of protein disulfide isomerase Trends Biochem. Sci. 9:438-441.
    • (1984) Trends Biochem. Sci. , vol.9 , pp. 438-441
    • Freedman, R.B.1
  • 22
    • 0024337857 scopus 로고
    • Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteins
    • Freedman, R. B. 1989 Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins. Cell 57:1069-1072.
    • (1989) Cell , vol.57 , pp. 1069-1072
    • Freedman, R.B.1
  • 25
    • 0023935921 scopus 로고
    • Characterization of a human cytomegalovirus glycoprotein complex (gel)
    • Gretch, D. R., R. C. Gehrz, and M. F. Stinski. 1988. Characterization of a human cytomegalovirus glycoprotein complex (gel). J Gen Virol. 69:1205-1215.
    • (1988) J Gen Virol. , vol.69 , pp. 1205-1215
    • Gretch, D.R.1    Gehrz, R.C.2    Stinski, M.F.3
  • 26
    • 0023108322 scopus 로고
    • Molecular biology and immunology of cytomegalovirus
    • Griffiths, P. D., and J. E. Grundy. 1987. Molecular biology and immunology of cytomegalovirus Biochem. J. 241:313-324.
    • (1987) Biochem. J. , vol.241 , pp. 313-324
    • Griffiths, P.D.1    Grundy, J.E.2
  • 27
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond, C., I. Braakman, and A. Helenius. 1994 Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control Proc Natl Acad Sci. USA 91:913-917
    • (1994) Proc Natl Acad Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 28
    • 0028076031 scopus 로고
    • Folding of VSV G protein: Sequential interaction with BiP and calnexin
    • Hammond, C., and A. Helenius. 1994. Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 266:456-458.
    • (1994) Science , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 29
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • Hammond, C., and A. Helenius. 1994. Quality control in the secretory pathway retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus J. Cell Biol. 126:41-52.
    • (1994) J. Cell Biol. , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 30
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius, A. 1994. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol Biol. Cell 5:253-265.
    • (1994) Mol Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 31
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick, J. P., and F.-U. Hartl. 1993 Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62:349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.-U.2
  • 32
    • 0026511275 scopus 로고
    • Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly
    • Hochstenbach, F., V. David, S. Watkins, and M. Brenner. 1992. Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T-and B-cell antigen receptors and major histocompatibility complex antigens during their assembly Proc. Natl. Acad. Sci. USA 89:4734-4738.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4734-4738
    • Hochstenbach, F.1    David, V.2    Watkins, S.3    Brenner, M.4
  • 33
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley, S. M., and A. Helenius. 1989. Protein oligomerization in the endoplasmic reticulum. Annu Rev. Cell Biol. 5:277-307.
    • (1989) Annu Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 34
    • 0028181429 scopus 로고
    • Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90)
    • Jackson, M. R., M. F. Cohen-Doyle, P.A. Peterson, and D. B. Williams. 1994. Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90). Science 263:384-387.
    • (1994) Science , vol.263 , pp. 384-387
    • Jackson, M.R.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Williams, D.B.4
  • 35
    • 0028801931 scopus 로고
    • Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum
    • Kim, P. S., and P. Arvan. 1995 Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J. Cell Biol. 128:29-38.
    • (1995) J. Cell Biol. , vol.128 , pp. 29-38
    • Kim, P.S.1    Arvan, P.2
  • 36
    • 0026656520 scopus 로고
    • Transient aggregation of nascent thyroglobulin in the endoplasmic reticulum: Relationship to the molecular chaperons, BiP
    • Kim, P. S., D. Bole, and P. Aryan. 1992. Transient aggregation of nascent thyroglobulin in the endoplasmic reticulum: relationship to the molecular chaperons, BiP. J. Cell Biol. 118:541-549.
    • (1992) J. Cell Biol. , vol.118 , pp. 541-549
    • Kim, P.S.1    Bole, D.2    Aryan, P.3
  • 37
    • 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
  • 39
    • 0028127183 scopus 로고
    • Prolonged association of temperature-sensitive mutants of human P-glyeoprotein with calnexin during biogenesis
    • Loo, T. W., and D. M. Clarke. 1994. Prolonged association of temperature-sensitive mutants of human P-glyeoprotein with calnexin during biogenesis. J Biol. Chem. 269:28683-28689.
    • (1994) J Biol. Chem. , vol.269 , pp. 28683-28689
    • Loo, T.W.1    Clarke, D.M.2
  • 40
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick, J. M., J. L. Dul, and Y. Argon. 1994. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum Nature (London) 370:373-375.
    • (1994) Nature (London) , vol.370 , pp. 373-375
    • Melnick, J.M.1    Dul, J.L.2    Argon, Y.3
  • 41
    • 0019508859 scopus 로고
    • Enhanced capacity of DNA repair in human cytomegalovirus-infected cells
    • Nishiyama, Y., and F. Rapp. 1981. Enhanced capacity of DNA repair in human cytomegalovirus-infected cells. J. Virol. 38:164-172.
    • (1981) J. Virol. , vol.38 , pp. 164-172
    • Nishiyama, Y.1    Rapp, F.2
  • 42
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • On, W.-J., P. H. Cameron, D. Y. Thomas, and J. J. M. Bergeron. 1993. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature (London) 364:771-776.
    • (1993) Nature (London) , vol.364 , pp. 771-776
    • On, W.-J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 43
    • 0021716895 scopus 로고
    • Polymorphism of human cytomegalovirus glycoproteins characterized by monoclonal antibodies
    • Pereira, L., M. Huffman, M. Tatsuno, and D. Dondero. 1984. Polymorphism of human cytomegalovirus glycoproteins characterized by monoclonal antibodies. Virology 139:73-86.
    • (1984) Virology , vol.139 , pp. 73-86
    • Pereira, L.1    Huffman, M.2    Tatsuno, M.3    Dondero, D.4
  • 44
    • 0019989495 scopus 로고
    • Cytotoxic T cells in cytomegalovirus infection: HLA restricted T-lymphocyte and non-T-lymphocyte cytotoxic responses correlate with recovery from cytomegalovinis infection in bone-marrow-transplant recipients
    • Quinnan, G. V., Jr., N. Kirmani, A. H. Rook, J. F. Manischewitz, L. Jackson, G. Moreschi, G. W. Santos, R. Saral, and W. H. Burns. 1982. Cytotoxic T cells in cytomegalovirus infection: HLA restricted T-lymphocyte and non-T-lymphocyte cytotoxic responses correlate with recovery from cytomegalovinis infection in bone-marrow-transplant recipients. N. Engl. J. Med 307:7-13.
    • (1982) N. Engl. J. Med , vol.307 , pp. 7-13
    • Quinnan Jr., G.V.1    Kirmani, N.2    Rook, A.H.3    Manischewitz, J.F.4    Jackson, L.5    Moreschi, G.6    Santos, G.W.7    Saral, R.8    Burns, W.H.9
  • 45
    • 0028147528 scopus 로고
    • Retention of unassembled components of integral membrane proteins by calnexin
    • Rajagopalan, S., Y. Xu, and M. B. Brenner. 1994. Retention of unassembled components of integral membrane proteins by calnexin. Science 263:387-390
    • (1994) Science , vol.263 , pp. 387-390
    • Rajagopalan, S.1    Xu, Y.2    Brenner, M.B.3
  • 46
    • 0023430549 scopus 로고
    • CD8-positive T lymphocytes specific for murine cytomegalo-virus immediate-early antigens mediate protective immunity
    • Reddehase, M. J., W. Mutter, K. Münch, H.-J. Bühring, and U. H. Koszinowski. 1987. CD8-positive T lymphocytes specific for murine cytomegalo-virus immediate-early antigens mediate protective immunity. J. Virol 61:3102-3108.
    • (1987) J. Virol , vol.61 , pp. 3102-3108
    • Reddehase, M.J.1    Mutter, W.2    Münch, K.3    Bühring, H.-J.4    Koszinowski, U.H.5
  • 47
    • 0022366849 scopus 로고
    • Interstitial murine cytomegalovirus pneumonia after irradiation: Characterization of cells that limit viral replication during established infection of the lungs
    • Reddehase, M. J., F. Weiland, K. Münch, S. Jonjic, A. Lüske, and U. H. Koszinowski. 1985. Interstitial murine cytomegalovirus pneumonia after irradiation: characterization of cells that limit viral replication during established infection of the lungs. J. Virol. 55:264-273.
    • (1985) J. Virol. , vol.55 , pp. 264-273
    • Reddehase, M.J.1    Weiland, F.2    Münch, K.3    Jonjic, S.4    Lüske, A.5    Koszinowski, U.H.6
  • 48
    • 0024149621 scopus 로고
    • Regulation of protein export from the endoplasmic reticulum
    • Rose, J. K., and R. W. Doms. 1988 Regulation of protein export from the endoplasmic reticulum. Annu Rev. Biol. 4:257-288.
    • (1988) Annu Rev. Biol. , vol.4 , pp. 257-288
    • Rose, J.K.1    Doms, R.W.2
  • 49
    • 0027455464 scopus 로고
    • Posttranslational folding of vesicular stomatitis virus G protein in the ER: Involvement of noncovalent and covalent complexes
    • Silva, A., I. Braakman, and A. Helenius. 1993. Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes. J. Cell Biol. 120:647-655.
    • (1993) J. Cell Biol. , vol.120 , pp. 647-655
    • Silva, A.1    Braakman, I.2    Helenius, A.3
  • 50
    • 0025907054 scopus 로고
    • The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosuphila rhudopsin
    • Stamnes, M. A., B.-H. Shieh, L. Chuman, G. L. Harris, and C. S. Zuker. 1991. The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosuphila rhudopsin. Cell 63:219-227
    • (1991) Cell , vol.63 , pp. 219-227
    • Stamnes, M.A.1    Shieh, B.-H.2    Chuman, L.3    Harris, G.L.4    Zuker, C.S.5
  • 51
    • 0017080733 scopus 로고
    • Human cytomegalovirus' glycoproteins associated with virions and dense bodies
    • Stinski, M. 1976. Human cytomegalovirus' glycoproteins associated with virions and dense bodies J. Virol. 19:594-609.
    • (1976) J. Virol. , vol.19 , pp. 594-609
    • Stinski, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.