메뉴 건너뛰기




Volumn 1, Issue , 2004, Pages

Evolution of the HIV-1 envelope glycoproteins with a disulfide bond between gp120 and gp41

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN; DISULFIDE;

EID: 4344717028     PISSN: 17424690     EISSN: None     Source Type: Journal    
DOI: 10.1186/1742-4690-1-3     Document Type: Article
Times cited : (32)

References (51)
  • 1
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • Colman PM, Lawrence MC: The structural biology of type I viral membrane fusion. Nat Rev Mol Cell Biol 2003, 4:309-319.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 2
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • Wyatt R, Sodroski J: The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 1998, 280:1884-1888.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 3
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert DM, Kim PS: Mechanisms of viral membrane fusion and its inhibition. Annu Rev Biochem 2001, 70:777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 7
    • 0000604395 scopus 로고    scopus 로고
    • The neutralizing antibody response to HIV-1: Viral evasion and escape from humoral immunity
    • Parren PWHI, Moore JP, Burton DR, Sattentau QJ: The neutralizing antibody response to HIV-1: viral evasion and escape from humoral immunity. AIDS 1999, 13 (Suppl. A):S137-S162.
    • (1999) AIDS , vol.13 , Issue.SUPPL. A
    • Parren, P.W.H.I.1    Moore, J.P.2    Burton, D.R.3    Sattentau, Q.J.4
  • 8
    • 0345369696 scopus 로고    scopus 로고
    • Human antibody responses to mature and immature forms of viral envelope in respiratory syncytial virus infection: Significance for subunit vaccines
    • Sakurai H, Williamson RA, Crowe JE, Beeler JA, Poignard P, Bastidas RB, Chanock RM, Burton DR: Human antibody responses to mature and immature forms of viral envelope in respiratory syncytial virus infection: significance for subunit vaccines. J Virol 1999, 73:2956-2962.
    • (1999) J. Virol. , vol.73 , pp. 2956-2962
    • Sakurai, H.1    Williamson, R.A.2    Crowe, J.E.3    Beeler, J.A.4    Poignard, P.5    Bastidas, R.B.6    Chanock, R.M.7    Burton, D.R.8
  • 9
    • 0033985999 scopus 로고    scopus 로고
    • A recombinant HIV-1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure
    • Binley JM, Sanders RW, Clas B, Schuelke N, Master A, Guo Y, Kajumo F, Anselma DJ, Maddon PJ, Olson WC, Moore JP: A recombinant HIV-1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure. J Virol 2000, 74:627-643.
    • (2000) J. Virol. , vol.74 , pp. 627-643
    • Binley, J.M.1    Sanders, R.W.2    Clas, B.3    Schuelke, N.4    Master, A.5    Guo, Y.6    Kajumo, F.7    Anselma, D.J.8    Maddon, P.J.9    Olson, W.C.10    Moore, J.P.11
  • 10
    • 0034063445 scopus 로고    scopus 로고
    • Variable-loop-deleted variants of the human immunodeficiency virus type 1 envelope glycoprotein can be stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits
    • Sanders RW, Schiffner L, Master A, Kajumo F, Guo Y, Dragic T, Moore JP, Binley JM: Variable-loop-deleted variants of the human immunodeficiency virus type 1 envelope glycoprotein can be stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits. J Virol 2000, 74:5091-5100.
    • (2000) J. Virol. , vol.74 , pp. 5091-5100
    • Sanders, R.W.1    Schiffner, L.2    Master, A.3    Kajumo, F.4    Guo, Y.5    Dragic, T.6    Moore, J.P.7    Binley, J.M.8
  • 11
    • 0038076112 scopus 로고    scopus 로고
    • Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions
    • Binley JM, Cayanan CS, Wiley C, Schulke N, Olson WC, Burton DR: Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions. J Virol 2003, 77:5678-5684.
    • (2003) J. Virol. , vol.77 , pp. 5678-5684
    • Binley, J.M.1    Cayanan, C.S.2    Wiley, C.3    Schulke, N.4    Olson, W.C.5    Burton, D.R.6
  • 12
    • 0037847545 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Env with an intersubunit disulfide bond engages coreceptors but requires bond reduction after engagement to induce fusion
    • Abrahamyan LG, Markosyan RM, Moore JP, Cohen FS, Melikyan GB: Human immunodeficiency virus type 1 Env with an intersubunit disulfide bond engages coreceptors but requires bond reduction after engagement to induce fusion. J Virol 2003, 77:5829-5836.
    • (2003) J. Virol. , vol.77 , pp. 5829-5836
    • Abrahamyan, L.G.1    Markosyan, R.M.2    Moore, J.P.3    Cohen, F.S.4    Melikyan, G.B.5
  • 13
    • 0142211253 scopus 로고    scopus 로고
    • Functional evolution of the HIV-1 envelope glycoprotein gp120-association site of gp41
    • Poumbourios P, Maerz AL, Drummer HE: Functional evolution of the HIV-1 envelope glycoprotein gp120-association site of gp41. J Biol Chem 2003, 278:42149-42160.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42149-42160
    • Poumbourios, P.1    Maerz, A.L.2    Drummer, H.E.3
  • 14
    • 0027499917 scopus 로고
    • Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein
    • Cao J, Bergeron L, Helseth E, Thali M, Repke H, Sodroski J: Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein. J Virol 1993, 67:2747-2755.
    • (1993) J. Virol. , vol.67 , pp. 2747-2755
    • Cao, J.1    Bergeron, L.2    Helseth, E.3    Thali, M.4    Repke, H.5    Sodroski, J.6
  • 15
    • 0028107566 scopus 로고
    • Functional role of the zipper motif region of human immunodeficiency virus type 1 transmembrane protein gp41
    • Chen SS: Functional role of the zipper motif region of human immunodeficiency virus type 1 transmembrane protein gp41. J Virol 1994, 68:2002-2010.
    • (1994) J. Virol. , vol.68 , pp. 2002-2010
    • Chen, S.S.1
  • 16
    • 0034984522 scopus 로고    scopus 로고
    • Functional analysis of the disulfide-bonded loop/chain reversal region of human immunodeficiency virus type 1 gp41 reveals a critical role in gp120-gp41 association
    • Maerz AL, Drummer HE, Wilson KA, Poumbourios P: Functional analysis of the disulfide-bonded loop/chain reversal region of human immunodeficiency virus type 1 gp41 reveals a critical role in gp120-gp41 association. J Virol 2001, 75:6635-6644.
    • (2001) J. Virol. , vol.75 , pp. 6635-6644
    • Maerz, A.L.1    Drummer, H.E.2    Wilson, K.A.3    Poumbourios, P.4
  • 17
    • 3843108323 scopus 로고    scopus 로고
    • Mutational analyses and natural variablility of the gp41 ectodomain
    • (Edited by: KuikenC, FoleyB, FreedE, HahnB, MarxP, McCutchanF, MellorsJ, WolinskyS and KorberB). Los Alamos, New Mexico, Los Alamos National Laboratory, Theoretical Biology and Biophysics Group
    • Sanders RW, Korber B, Lu M, Berkhout B, Moore JP: Mutational analyses and natural variablility of the gp41 ectodomain. HIV Sequence compendium 2002 (Edited by: KuikenC, FoleyB, FreedE, HahnB, MarxP, McCutchanF, MellorsJ, WolinskyS and KorberB). Los Alamos, New Mexico, Los Alamos National Laboratory, Theoretical Biology and Biophysics Group 2002, 43-68.
    • (2002) HIV Sequence Compendium 2002 , pp. 43-68
    • Sanders, R.W.1    Korber, B.2    Lu, M.3    Berkhout, B.4    Moore, J.P.5
  • 18
    • 0035978480 scopus 로고    scopus 로고
    • Model for the structure of the HIV gp41 ectodomain: Insight into the intermolecular interactions of the gp41 loop
    • Caffrey M: Model for the structure of the HIV gp41 ectodomain: insight into the intermolecular interactions of the gp41 loop. Biochim Biophys Acta 2001, 1536:116-122.
    • (2001) Biochim. Biophys. Acta , vol.1536 , pp. 116-122
    • Caffrey, M.1
  • 20
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, Kim PS: Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997, 89:263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 21
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan K, Liu J, Wang J, Shen S, Lu M: Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc Natl Acad Sci USA 1997, 94:12303-12308.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3    Shen, S.4    Lu, M.5
  • 23
    • 0023935921 scopus 로고
    • Characterization of a human cytomegalovirus glycoprotein complex (gcI)
    • Gretch DR, Gehrz RC, Stinski MF: Characterization of a human cytomegalovirus glycoprotein complex (gcI). J Gen Virol 1988, 69 ( Pt 6):1205-1215.
    • (1988) J. Gen. Virol. , vol.69 , Issue.PART 6 , pp. 1205-1215
    • Gretch, D.R.1    Gehrz, R.C.2    Stinski, M.F.3
  • 24
    • 0020658446 scopus 로고
    • Respiratory syncytial virus polypeptides. III. The envelope-associated proteins
    • Gruber C, Levine S: Respiratory syncytial virus polypeptides. III. The envelope-associated proteins. J Gen Virol 1983, 64 (Pt 4):825-832.
    • (1983) J. Gen. Virol. , vol.64 , Issue.PART 4 , pp. 825-832
    • Gruber, C.1    Levine, S.2
  • 25
    • 0017839313 scopus 로고
    • Glycoproteins of measles virus under reducing and nonreducing conditions
    • Hardwick JM, Bussell RH: Glycoproteins of measles virus under reducing and nonreducing conditions. J Virol 1978, 25:687-692.
    • (1978) J. Virol. , vol.25 , pp. 687-692
    • Hardwick, J.M.1    Bussell, R.H.2
  • 26
    • 0017159301 scopus 로고
    • Subunit structure of the glycoprotein complex of avian tumor virus
    • Leamnson RN, Halpern MS: Subunit structure of the glycoprotein complex of avian tumor virus. J Virol 1976, 18:956-968.
    • (1976) J. Virol. , vol.18 , pp. 956-968
    • Leamnson, R.N.1    Halpern, M.S.2
  • 27
    • 0017352589 scopus 로고
    • A structural protein complex in Moloney leukemia virus
    • Leamnson RN, Shander MH, Halpern MS: A structural protein complex in Moloney leukemia virus. Virol 1977, 76:437-439.
    • (1977) Virol. , vol.76 , pp. 437-439
    • Leamnson, R.N.1    Shander, M.H.2    Halpern, M.S.3
  • 28
    • 0024599232 scopus 로고
    • Identification of the gB homologues of equine herpesvirus types 1 and 4 as disulphide-linked heterodimers and their characterization using monoclonal antibodies
    • Meredith DM, Stocks JM, Whittaker GR, Halliburton IW, Snowden BW, Killington RA: Identification of the gB homologues of equine herpesvirus types 1 and 4 as disulphide-linked heterodimers and their characterization using monoclonal antibodies. J Gen Virol 1989, 70 ( Pt 5):1161-1172.
    • (1989) J. Gen. Virol. , vol.70 , Issue.PART 5 , pp. 1161-1172
    • Meredith, D.M.1    Stocks, J.M.2    Whittaker, G.R.3    Halliburton, I.W.4    Snowden, B.W.5    Killington, R.A.6
  • 29
    • 0017837785 scopus 로고
    • An analysis of type-C retrovirus polypeptides and their associations in the virion
    • Montelaro RC, Sullivan SJ, Bolognesi DP: An analysis of type-C retrovirus polypeptides and their associations in the virion. Virol 1978, 84:19-31.
    • (1978) Virol. , vol.84 , pp. 19-31
    • Montelaro, R.C.1    Sullivan, S.J.2    Bolognesi, D.P.3
  • 30
    • 0031927203 scopus 로고    scopus 로고
    • Moloney murine leukemia virus envelope protein subunits, gp70 and Pr15E, form a stable disulfide-linked complex
    • Opstelten DJ, Wallin M, Garoff H: Moloney murine leukemia virus envelope protein subunits, gp70 and Pr15E, form a stable disulfide-linked complex. J Virol 1998, 72:6537-6545.
    • (1998) J. Virol. , vol.72 , pp. 6537-6545
    • Opstelten, D.J.1    Wallin, M.2    Garoff, H.3
  • 31
    • 0017719251 scopus 로고
    • The presence of disulfide-linked gp70-p15(E) complexes in AKR murine leukemia virus
    • Pinter A, Fleissner E: The presence of disulfide-linked gp70-p15(E) complexes in AKR murine leukemia virus. Virol 1977, 83:417-422.
    • (1977) Virol. , vol.83 , pp. 417-422
    • Pinter, A.1    Fleissner, E.2
  • 32
    • 0018742151 scopus 로고
    • Structural studies of retroviruses: Characterization of oligomeric complexes of murine and feline leukemia virus envelope and core components formed upon cross-linking
    • Pinter A, Fleissner E: Structural studies of retroviruses: characterization of oligomeric complexes of murine and feline leukemia virus envelope and core components formed upon cross-linking. J Virol 1979, 30:157-165.
    • (1979) J. Virol. , vol.30 , pp. 157-165
    • Pinter, A.1    Fleissner, E.2
  • 33
    • 0020513951 scopus 로고
    • Comparison of structural domains of gp70s of ecotropic Akv and dualtropic MCF-247 MuLVs
    • Pinter A, Honnen WJ: Comparison of structural domains of gp70s of ecotropic Akv and dualtropic MCF-247 MuLVs. Virol 1983, 129:40-50.
    • (1983) Virol. , vol.129 , pp. 40-50
    • Pinter, A.1    Honnen, W.J.2
  • 34
    • 0021331590 scopus 로고
    • Characterization of structural and immunological properties of specific domains of Friend ecotropic and dual-tropic murine leukemia virus gp70s
    • Pinter A, Honnen WJ: Characterization of structural and immunological properties of specific domains of Friend ecotropic and dual-tropic murine leukemia virus gp70s. J Virol 1984, 49:452-458.
    • (1984) J. Virol. , vol.49 , pp. 452-458
    • Pinter, A.1    Honnen, W.J.2
  • 35
    • 0017404533 scopus 로고
    • Two disulfide-linked polypeptide chains constitute the active F protein of paramyxoviruses
    • Scheid A, Choppin PW: Two disulfide-linked polypeptide chains constitute the active F protein of paramyxoviruses. Virol 1977, 80:54-66.
    • (1977) Virol. , vol.80 , pp. 54-66
    • Scheid, A.1    Choppin, P.W.2
  • 36
    • 0021686786 scopus 로고
    • Structural characterization of virion proteins and genomic RNA of human parainfluenza virus 3
    • Storey DG, Dimock K, Kang CY: Structural characterization of virion proteins and genomic RNA of human parainfluenza virus 3. J Virol 1984, 52:761-766.
    • (1984) J. Virol. , vol.52 , pp. 761-766
    • Storey, D.G.1    Dimock, K.2    Kang, C.Y.3
  • 37
    • 0022481619 scopus 로고
    • Synthesis and processing of bovine herpesvirus 1 glycoproteins
    • Hurk van Drunen Littel-van den, Babiuk LA: Synthesis and processing of bovine herpesvirus 1 glycoproteins. J Virol 1986, 59:401-410.
    • (1986) J. Virol. , vol.59 , pp. 401-410
    • van Drunen Littel-van den, H.1    Babiuk, L.A.2
  • 38
    • 0019451160 scopus 로고
    • Disulphide bonds of haemagglutinin of Asian influenza virus
    • Waterfield M, Scrace G, Skehel J: Disulphide bonds of haemagglutinin of Asian influenza virus. Nature 1981, 289:422-424.
    • (1981) Nature , vol.289 , pp. 422-424
    • Waterfield, M.1    Scrace, G.2    Skehel, J.3
  • 39
    • 0020626190 scopus 로고
    • Immunochemical identification of rubella virus hemagglutinin
    • Waxham MN, Wolinsky JS: Immunochemical identification of rubella virus hemagglutinin. Virol 1983, 126:194-203.
    • (1983) Virol. , vol.126 , pp. 194-203
    • Waxham, M.N.1    Wolinsky, J.S.2
  • 40
    • 0017359935 scopus 로고
    • Cellular maturation of oncornavirus glycoproteins: Topological arrangement of precursor and product forms in cellular membranes
    • Witte ON, Tsukamoto-Adey A, Weissman IL: Cellular maturation of oncornavirus glycoproteins: topological arrangement of precursor and product forms in cellular membranes. Virol 1977, 76:539-553.
    • (1977) Virol. , vol.76 , pp. 539-553
    • Witte, O.N.1    Tsukamoto-Adey, A.2    Weissman, I.L.3
  • 41
    • 0035815637 scopus 로고    scopus 로고
    • HIV-1 RNA editing, hypermutation and error-prone reverse transcription
    • Berkhout B, Das AT, Beerens N: HIV-1 RNA editing, hypermutation and error-prone reverse transcription. Science 2001, 292:7.
    • (2001) Science , vol.292 , pp. 7
    • Berkhout, B.1    Das, A.T.2    Beerens, N.3
  • 44
    • 0026098303 scopus 로고
    • Differential loss of envelope glycoprotein gp120 from virions of human immunodeficiency virus type 1 isolates: Effects on infectivity and neutralization
    • McKeating JA, McKnight A, Moore JP: Differential loss of envelope glycoprotein gp120 from virions of human immunodeficiency virus type 1 isolates: effects on infectivity and neutralization. J Virol 1991, 65:852-860.
    • (1991) J. Virol. , vol.65 , pp. 852-860
    • McKeating, J.A.1    McKnight, A.2    Moore, J.P.3
  • 45
    • 0025572710 scopus 로고
    • Dissociation of gp120 from HIV-1 virions induced by soluble CD4
    • Moore JP, McKeating JA, Weiss RA, Sattentau QJ: Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science 1990, 250:1139-1142.
    • (1990) Science , vol.250 , pp. 1139-1142
    • Moore, J.P.1    McKeating, J.A.2    Weiss, R.A.3    Sattentau, Q.J.4
  • 46
    • 0026318224 scopus 로고
    • Changes in growth properties on passage in tissue culture of viruses derived from infectious molecular clones of HIV-1LAI, HIV-1MAL, and HIV-1ELI
    • Peden K, Emerman M, Montagnier L: Changes in growth properties on passage in tissue culture of viruses derived from infectious molecular clones of HIV-1LAI, HIV-1MAL, and HIV-1ELI. Virol 1991, 185:661-672.
    • (1991) Virol. , vol.185 , pp. 661-672
    • Peden, K.1    Emerman, M.2    Montagnier, L.3
  • 47
    • 0036314488 scopus 로고    scopus 로고
    • Differential transmission of human immunodeficiency virus type 1 by distinct subsets of effector dendritic cells
    • Sanders RW, de Jong EC, Baldwin CE, Schuitemaker JH, Kapsenberg ML, Berkhout B: Differential transmission of human immunodeficiency virus type 1 by distinct subsets of effector dendritic cells. J Virol 2002, 76:7812-7821.
    • (2002) J. Virol. , vol.76 , pp. 7812-7821
    • Sanders, R.W.1    de Jong, E.C.2    Baldwin, C.E.3    Schuitemaker, J.H.4    Kapsenberg, M.L.5    Berkhout, B.6
  • 48
    • 0032889526 scopus 로고    scopus 로고
    • A hairpin structure in the R region of the Human Immunodeficiency Virus type 1 RNA genome is instrumental in polyadenylation site selection
    • Das AT, Klaver B, Berkhout B: A hairpin structure in the R region of the Human Immunodeficiency Virus type 1 RNA genome is instrumental in polyadenylation site selection. J Virol 1999, 73:81-91.
    • (1999) J. Virol. , vol.73 , pp. 81-91
    • Das, A.T.1    Klaver, B.2    Berkhout, B.3
  • 49
  • 50
    • 0034255169 scopus 로고    scopus 로고
    • LuSIV cells: A reporter cell line for the detection and quantitation of a single cycle of HIV and SIV replication
    • Roos JW, Maughan MF, Liao Z, Hildreth JE, Clements JE: LuSIV cells: a reporter cell line for the detection and quantitation of a single cycle of HIV and SIV replication. Virol 2000, 273:307-315.
    • (2000) Virol. , vol.273 , pp. 307-315
    • Roos, J.W.1    Maughan, M.F.2    Liao, Z.3    Hildreth, J.E.4    Clements, J.E.5
  • 51
    • 0031055285 scopus 로고    scopus 로고
    • A conserved hairpin motif in the R-U5 region of the human immunodeficiency virus type 1 RNA genome is essential for replication
    • Das AT, Klaver B, Klasens BIF, van Wamel JLB, Berkhout B: A conserved hairpin motif in the R-U5 region of the human immunodeficiency virus type 1 RNA genome is essential for replication. J Virol 1997, 71:2346-2356.
    • (1997) J. Virol. , vol.71 , pp. 2346-2356
    • Das, A.T.1    Klaver, B.2    Klasens, B.I.F.3    van Wamel, J.L.B.4    Berkhout, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.