메뉴 건너뛰기




Volumn 394, Issue 4, 2010, Pages 904-908

Role for the disulfide-bonded region of human immunodeficiency virus type 1 gp41 in receptor-triggered activation of membrane fusion function

Author keywords

Disulfide bonded region; gp41; HIV 1; Membrane fusion; Receptor

Indexed keywords

CD4 ANTIGEN; CHEMOKINE RECEPTOR; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41;

EID: 77950867623     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.03.071     Document Type: Article
Times cited : (10)

References (35)
  • 2
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta R.A., Wild C.T., Weng Y., and Weiss C.D. Capture of an early fusion-active conformation of HIV-1 gp41. Nat. Struct. Biol. 5 (1998) 276-279
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 3
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan D.C., Fass D., Berger J.M., and Kim P.S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89 (1997) 263-273
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 5
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan K., Liu J., Wang J., Shen S., and Lu M. Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. USA 94 (1997) 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
  • 6
    • 59849107898 scopus 로고    scopus 로고
    • Common principles and intermediates of viral protein-mediated fusion: the HIV-1 paradigm
    • Melikyan G.B. Common principles and intermediates of viral protein-mediated fusion: the HIV-1 paradigm. Retrovirology 5 (2008) 111
    • (2008) Retrovirology , vol.5 , pp. 111
    • Melikyan, G.B.1
  • 7
    • 0038076112 scopus 로고    scopus 로고
    • Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions
    • Binley J.M., Cayanan C.S., Wiley C., Schulke N., Olson W.C., and Burton D.R. Redox-triggered infection by disulfide-shackled human immunodeficiency virus type 1 pseudovirions. J. Virol. 77 (2003) 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
  • 8
    • 0026069632 scopus 로고
    • Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein
    • Helseth E., Olshevsky U., Furman C., and Sodroski J. Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein. J. Virol. 65 (1991) 2119-2123
    • (1991) J. Virol. , vol.65 , pp. 2119-2123
    • Helseth, E.1    Olshevsky, U.2    Furman, C.3    Sodroski, J.4
  • 9
    • 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 A.L., Drummer H.E., Wilson K.A., and 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. 75 (2001) 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
  • 10
    • 0142211253 scopus 로고    scopus 로고
    • Functional evolution of the HIV-1 envelope glycoprotein 120 association site of glycoprotein 41
    • Poumbourios P., Maerz A.L., and Drummer H.E. Functional evolution of the HIV-1 envelope glycoprotein 120 association site of glycoprotein 41. J. Biol. Chem. 278 (2003) 42149-42160
    • (2003) J. Biol. Chem. , vol.278 , pp. 42149-42160
    • Poumbourios, P.1    Maerz, A.L.2    Drummer, H.E.3
  • 11
    • 0028801450 scopus 로고
    • Epitope exposure on functional, oligomeric HIV-1 gp41 molecules
    • Sattentau Q.J., Zolla-Pazner S., and Poignard P. Epitope exposure on functional, oligomeric HIV-1 gp41 molecules. Virology 206 (1995) 713-717
    • (1995) Virology , vol.206 , pp. 713-717
    • Sattentau, Q.J.1    Zolla-Pazner, S.2    Poignard, P.3
  • 12
    • 0036889127 scopus 로고    scopus 로고
    • Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion
    • Finnegan C.M., Berg W., Lewis G.K., and DeVico A.L. Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion. J. Virol. 76 (2002) 12123-12134
    • (2002) J. Virol. , vol.76 , pp. 12123-12134
    • Finnegan, C.M.1    Berg, W.2    Lewis, G.K.3    DeVico, A.L.4
  • 14
    • 2942624406 scopus 로고    scopus 로고
    • Expression and biochemical analysis of the entire HIV-2 gp41 ectodomain: determinants of stability map to N- and C-terminal sequences outside the 6-helix bundle core
    • Lay C.-S., Wilson K.A., Kobe B., Kemp B.E., Drummer H.E., and Poumbourios P. Expression and biochemical analysis of the entire HIV-2 gp41 ectodomain: determinants of stability map to N- and C-terminal sequences outside the 6-helix bundle core. FEBS Lett. 567 (2004) 183-188
    • (2004) FEBS Lett. , vol.567 , pp. 183-188
    • Lay, C.-S.1    Wilson, K.A.2    Kobe, B.3    Kemp, B.E.4    Drummer, H.E.5    Poumbourios, P.6
  • 15
    • 0028842207 scopus 로고
    • Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes
    • Connor R.I., Chen B.K., Choe S., and Landau N.R. Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes. Virology 206 (1995) 935-944
    • (1995) Virology , vol.206 , pp. 935-944
    • Connor, R.I.1    Chen, B.K.2    Choe, S.3    Landau, N.R.4
  • 17
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • Graham F.L., and van der Eb A.J. A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology 52 (1973) 456-467
    • (1973) Virology , vol.52 , pp. 456-467
    • Graham, F.L.1    van der Eb, A.J.2
  • 18
    • 34548170245 scopus 로고    scopus 로고
    • Functional links between the fusion peptide-proximal polar segment and membrane-proximal region of human immunodeficiency virus gp41 in distinct phases of membrane fusion
    • Bellamy-McIntyre A.K., Lay C.S., Bär S., Maerz A.L., Talbo G.H., Drummer H.E., and Poumbourios P. Functional links between the fusion peptide-proximal polar segment and membrane-proximal region of human immunodeficiency virus gp41 in distinct phases of membrane fusion. J. Biol. Chem. 282 (2007) 23104-23116
    • (2007) J. Biol. Chem. , vol.282 , pp. 23104-23116
    • Bellamy-McIntyre, A.K.1    Lay, C.S.2    Bär, S.3    Maerz, A.L.4    Talbo, G.H.5    Drummer, H.E.6    Poumbourios, P.7
  • 19
    • 0346688617 scopus 로고    scopus 로고
    • Role of the ectodomain of the gp41 transmembrane envelope protein of human immunodeficiency virus type 1 in late steps of the membrane fusion process
    • Bär S., and Alizon M. Role of the ectodomain of the gp41 transmembrane envelope protein of human immunodeficiency virus type 1 in late steps of the membrane fusion process. J. Virol. 78 (2004) 811-820
    • (2004) J. Virol. , vol.78 , pp. 811-820
    • Bär, S.1    Alizon, M.2
  • 21
    • 0027081957 scopus 로고
    • Antibody epitopes sensitive to the state of human immunodeficiency virus type 1 gp41 oligomerization map to a putative alpha-helical region
    • Poumbourios P., McPhee D.A., and Kemp B.E. Antibody epitopes sensitive to the state of human immunodeficiency virus type 1 gp41 oligomerization map to a putative alpha-helical region. AIDS Res. Hum. Retroviruses 8 (1992) 2055-2062
    • (1992) AIDS Res. Hum. Retroviruses , vol.8 , pp. 2055-2062
    • Poumbourios, P.1    McPhee, D.A.2    Kemp, B.E.3
  • 23
    • 0029836434 scopus 로고    scopus 로고
    • Increased envelope spike density and stability are not required for the neutralization resistance of primary human immunodeficiency viruses
    • Karlsson G.B., Gao F., Robinson J., Hahn B., and Sodroski J. Increased envelope spike density and stability are not required for the neutralization resistance of primary human immunodeficiency viruses. J. Virol. 70 (1996) 6136-6142
    • (1996) J. Virol. , vol.70 , pp. 6136-6142
    • Karlsson, G.B.1    Gao, F.2    Robinson, J.3    Hahn, B.4    Sodroski, J.5
  • 25
    • 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 L.G., Markosyan R.M., Moore J.P., Cohen F.S., and Melikyan G.B. Human immunodeficiency virus type 1 Env with an intersubunit disulfide bond engages coreceptors but requires bond reduction after engagement to induce fusion. J. Virol. 77 (2003) 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
  • 26
    • 0035163480 scopus 로고    scopus 로고
    • Conserved, N-linked carbohydrates of human immunodeficiency virus type 1 gp41 are largely dispensable for viral replication
    • Johnson W.E., Sauvron J.M., and Desrosiers R.C. Conserved, N-linked carbohydrates of human immunodeficiency virus type 1 gp41 are largely dispensable for viral replication. J. Virol. 75 (2001) 11426-11436
    • (2001) J. Virol. , vol.75 , pp. 11426-11436
    • Johnson, W.E.1    Sauvron, J.M.2    Desrosiers, R.C.3
  • 27
    • 0026579886 scopus 로고
    • Mutational analysis of conserved N-linked glycosylation sites of human immunodeficiency virus type 1 gp41
    • Lee W.R., Yu X.F., Syu W.J., Essex M., and Lee T.H. Mutational analysis of conserved N-linked glycosylation sites of human immunodeficiency virus type 1 gp41. J. Virol. 66 (1992) 1799-1803
    • (1992) J. Virol. , vol.66 , pp. 1799-1803
    • Lee, W.R.1    Yu, X.F.2    Syu, W.J.3    Essex, M.4    Lee, T.H.5
  • 29
    • 47049126218 scopus 로고    scopus 로고
    • Intersubunit disulfide isomerization controls membrane fusion of human T-cell leukemia virus Env
    • Li K., Zhang S., Kronqvist M., Wallin M., Ekstrom M., Derse D., and Garoff H. Intersubunit disulfide isomerization controls membrane fusion of human T-cell leukemia virus Env. J. Virol. 82 (2008) 7135-7143
    • (2008) J. Virol. , vol.82 , pp. 7135-7143
    • Li, K.1    Zhang, S.2    Kronqvist, M.3    Wallin, M.4    Ekstrom, M.5    Derse, D.6    Garoff, H.7
  • 30
    • 0842307062 scopus 로고    scopus 로고
    • Isomerization of the intersubunit disulphide-bond in Env controls retrovirus fusion
    • Wallin M., Ekstrom M., and Garoff H. Isomerization of the intersubunit disulphide-bond in Env controls retrovirus fusion. EMBO J. 23 (2004) 54-65
    • (2004) EMBO J. , vol.23 , pp. 54-65
    • Wallin, M.1    Ekstrom, M.2    Garoff, H.3
  • 31
    • 0033920211 scopus 로고    scopus 로고
    • Functional implications of the human T-lymphotropic virus type 1 transmembrane glycoprotein helical hairpin structure
    • Maerz A.L., Center R.J., Kemp B.E., Kobe B., and Poumbourios P. Functional implications of the human T-lymphotropic virus type 1 transmembrane glycoprotein helical hairpin structure. J. Virol. 74 (2000) 6614-6621
    • (2000) J. Virol. , vol.74 , pp. 6614-6621
    • Maerz, A.L.1    Center, R.J.2    Kemp, B.E.3    Kobe, B.4    Poumbourios, P.5
  • 32
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong P.D., Wyatt R., Robinson J., Sweet R.W., Sodroski J., and Hendrickson W.A. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393 (1998) 648-659
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 33
  • 34
    • 18644375565 scopus 로고    scopus 로고
    • Structural and immunological characterisation of heteroclitic peptide analogues corresponding to the 600-612 region of the HIV envelope gp41 glycoprotein
    • Du A.P., Limal D., Semetey V., Dali H., Jolivet M., Desgranges C., Cung M.T., Briand J.P., Petit M.C., and Muller S. Structural and immunological characterisation of heteroclitic peptide analogues corresponding to the 600-612 region of the HIV envelope gp41 glycoprotein. J. Mol. Biol. 323 (2002) 503-521
    • (2002) J. Mol. Biol. , vol.323 , pp. 503-521
    • Du, A.P.1    Limal, D.2    Semetey, V.3    Dali, H.4    Jolivet, M.5    Desgranges, C.6    Cung, M.T.7    Briand, J.P.8    Petit, M.C.9    Muller, S.10
  • 35
    • 0033985999 scopus 로고    scopus 로고
    • A recombinant human immunodeficiency virus type 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 J.M., Sanders R.W., Clas B., Schuelke N., Master A., Guo Y., Kajumo F., Anselma D.J., Maddon P.J., Olson W.C., and Moore J.P. A recombinant human immunodeficiency virus type 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. 74 (2000) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.