메뉴 건너뛰기




Volumn 583, Issue 7, 2009, Pages 1201-1206

Effects of mutations on HIV-1 infectivity and neutralization involving the conserved NNNT amino acid sequence in the gp120 V3 loop

Author keywords

HIV; N linked glycosylation; Neutralization; V3 loop; Viral infectivity

Indexed keywords

GLYCOPROTEIN GP 120; NEUTRALIZING ANTIBODY;

EID: 62849099645     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.03.010     Document Type: Article
Times cited : (6)

References (30)
  • 1
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard C.K., Spellman M.W., Riddle L., Harris R.J., Thomas J.N., and Gregory T.J. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J. Biol. Chem. 265 (1990) 10373-10382
    • (1990) J. Biol. Chem. , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 2
    • 0028244285 scopus 로고
    • An N-glycan within the human immunodeficiency virus type 1 gp120 V3 loop affects virus neutralization
    • Back N.K., Smit L., De Jong J.J., Keulen W., Schutten M., Goudsmit J., and Tersmette M. An N-glycan within the human immunodeficiency virus type 1 gp120 V3 loop affects virus neutralization. Virology 199 (1994) 431-438
    • (1994) Virology , vol.199 , pp. 431-438
    • Back, N.K.1    Smit, L.2    De Jong, J.J.3    Keulen, W.4    Schutten, M.5    Goudsmit, J.6    Tersmette, M.7
  • 3
    • 0029940696 scopus 로고    scopus 로고
    • Rapid selection for an N-linked oligosaccharide by monoclonal antibodies directed against the V3 loop of human immunodeficiency virus type 1
    • Schonning K., Jansson B., Olofsson S., and Hansen J.E. Rapid selection for an N-linked oligosaccharide by monoclonal antibodies directed against the V3 loop of human immunodeficiency virus type 1. J. Gen. Virol. 77 (1996) 753-758
    • (1996) J. Gen. Virol. , vol.77 , pp. 753-758
    • Schonning, K.1    Jansson, B.2    Olofsson, S.3    Hansen, J.E.4
  • 4
    • 0036935266 scopus 로고    scopus 로고
    • The N-linked glycan g15 within the V3 loop of the HIV-1 external glycoprotein gp120 affects coreceptor usage, cellular tropism, and neutralization
    • Polzer S., Dittmar M.T., Schmitz H., and Schreiber M. The N-linked glycan g15 within the V3 loop of the HIV-1 external glycoprotein gp120 affects coreceptor usage, cellular tropism, and neutralization. Virology 304 (2002) 70-80
    • (2002) Virology , vol.304 , pp. 70-80
    • Polzer, S.1    Dittmar, M.T.2    Schmitz, H.3    Schreiber, M.4
  • 11
    • 62849118476 scopus 로고    scopus 로고
    • Human Retroviruses and AIDS 1999: A Compilation and Analysis of Nucleic Acid and Amino Acid Sequences. Part VII: Global Variation in the HIV-1 V3 Region (Kuiken, C.L., Foley B., Hahn, B., Marx, P.A., McCutchan, F., Mellors, J.W., Mullins, J.I., Wolinsky, S., and Korber, B., Eds.). Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, NM.
    • Human Retroviruses and AIDS 1999: A Compilation and Analysis of Nucleic Acid and Amino Acid Sequences. Part VII: Global Variation in the HIV-1 V3 Region (Kuiken, C.L., Foley B., Hahn, B., Marx, P.A., McCutchan, F., Mellors, J.W., Mullins, J.I., Wolinsky, S., and Korber, B., Eds.). Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, NM.
  • 12
    • 0036771699 scopus 로고    scopus 로고
    • Sequence variation and consensus sequence of V3 loop on HIV-1 gp120
    • Tian H., Lan C., and Chen Y.H. Sequence variation and consensus sequence of V3 loop on HIV-1 gp120. Immunol. Lett. 83 (2002) 231-233
    • (2002) Immunol. Lett. , vol.83 , pp. 231-233
    • Tian, H.1    Lan, C.2    Chen, Y.H.3
  • 13
  • 14
    • 0032991878 scopus 로고    scopus 로고
    • The N-linked glycan of the V3 region of HIV-1 gp120 and CXCR4-dependent multiplication of a human immunodeficiency virus type 1 lymphocyte-tropic variant
    • Losman B., Biller M., Olofsson S., Schønning K., Lund O.S., Svennerholm B., Hansen J.E., and Bolmstedt A. The N-linked glycan of the V3 region of HIV-1 gp120 and CXCR4-dependent multiplication of a human immunodeficiency virus type 1 lymphocyte-tropic variant. FEBS Lett. 454 (1999) 47-52
    • (1999) FEBS Lett. , vol.454 , pp. 47-52
    • Losman, B.1    Biller, M.2    Olofsson, S.3    Schønning, K.4    Lund, O.S.5    Svennerholm, B.6    Hansen, J.E.7    Bolmstedt, A.8
  • 15
    • 1842562419 scopus 로고    scopus 로고
    • N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies
    • McCaffrey R.A., Saunders C., Hensel M., and Stamatatos L. N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies. J. Virol. 78 (2004) 3279-3295
    • (2004) J. Virol. , vol.78 , pp. 3279-3295
    • McCaffrey, R.A.1    Saunders, C.2    Hensel, M.3    Stamatatos, L.4
  • 17
    • 33644609596 scopus 로고    scopus 로고
    • CCR5 use by human immunodeficiency virus type 1 is associated closely with the gp120 V3 loop N-linked glycosylation site
    • Clevestig P., Pramanik L., Leitner T., and Ehrnst A. CCR5 use by human immunodeficiency virus type 1 is associated closely with the gp120 V3 loop N-linked glycosylation site. J. Gen. Virol. 87 (2006) 607-612
    • (2006) J. Gen. Virol. , vol.87 , pp. 607-612
    • Clevestig, P.1    Pramanik, L.2    Leitner, T.3    Ehrnst, A.4
  • 18
    • 0034469170 scopus 로고    scopus 로고
    • The N-terminal V3 loop glycan modulates the interaction of clade A and B human immunodeficiency virus type 1 envelopes with CD4 and chemokine receptors
    • Malenbaum S.E., Yang D., Cavacini L., Posner M., Robinson J., and Cheng-Mayer C. The N-terminal V3 loop glycan modulates the interaction of clade A and B human immunodeficiency virus type 1 envelopes with CD4 and chemokine receptors. J. Virol. 74 (2000) 11008-11016
    • (2000) J. Virol. , vol.74 , pp. 11008-11016
    • Malenbaum, S.E.1    Yang, D.2    Cavacini, L.3    Posner, M.4    Robinson, J.5    Cheng-Mayer, C.6
  • 19
    • 0037515376 scopus 로고    scopus 로고
    • Antibody neutralization of human immunodeficiency virus type 1 (HIV-1)
    • Schønning K. Antibody neutralization of human immunodeficiency virus type 1 (HIV-1). APMIS Suppl. 111 (2003) 1-42
    • (2003) APMIS Suppl. , vol.111 , pp. 1-42
    • Schønning, K.1
  • 20
    • 33748881797 scopus 로고    scopus 로고
    • N-Glycans in the gp120 V1/V2 domain of the HIV-1 strain NL4-3 are indispensable for viral infectivity and resistance against antibody neutralization
    • Wolk T., and Schreiber M. N-Glycans in the gp120 V1/V2 domain of the HIV-1 strain NL4-3 are indispensable for viral infectivity and resistance against antibody neutralization. Med. Microbiol. Immunol. 195 (2006) 165-172
    • (2006) Med. Microbiol. Immunol. , vol.195 , pp. 165-172
    • Wolk, T.1    Schreiber, M.2
  • 21
    • 0141458878 scopus 로고    scopus 로고
    • Assorted mutations in the envelope gene of simian immunodeficiency virus lead to loss of neutralization resistance against antibodies representing a broad spectrum of specificities
    • Johnson W.E., Sanford H., Schwall L., Burton D.R., Parren P.W., Robinson J.E., and Desrosiers R.C. Assorted mutations in the envelope gene of simian immunodeficiency virus lead to loss of neutralization resistance against antibodies representing a broad spectrum of specificities. J. Virol. 77 (2003) 9993-10003
    • (2003) J. Virol. , vol.77 , pp. 9993-10003
    • Johnson, W.E.1    Sanford, H.2    Schwall, L.3    Burton, D.R.4    Parren, P.W.5    Robinson, J.E.6    Desrosiers, R.C.7
  • 22
    • 0028229817 scopus 로고
    • Antibodies of symptomatic human immunodeficiency virus type 1-infected individuals are directed to the V3 domain of noninfectious and not of infectious virions present in autologous serum
    • Schreiber M., Petersen H., Wachsmuth C., Müller H., Hufert F.T., and Schmitz H. Antibodies of symptomatic human immunodeficiency virus type 1-infected individuals are directed to the V3 domain of noninfectious and not of infectious virions present in autologous serum. J. Virol. 68 (1994) 3908-3916
    • (1994) J. Virol. , vol.68 , pp. 3908-3916
    • Schreiber, M.1    Petersen, H.2    Wachsmuth, C.3    Müller, H.4    Hufert, F.T.5    Schmitz, H.6
  • 23
    • 0023706667 scopus 로고
    • Monoclonal antibodies directed against human immunodeficiency virus (HIV) gag proteins with specificity for conserved epitopes in HIV-1, HIV-2 and simian immunodeficiency virus
    • Niedrig M., Rabanus J.P., L'Age Stehr J., Gelderblom H.R., and Pauli G. Monoclonal antibodies directed against human immunodeficiency virus (HIV) gag proteins with specificity for conserved epitopes in HIV-1, HIV-2 and simian immunodeficiency virus. J. Gen. Virol. 69 (1988) 2109-2114
    • (1988) J. Gen. Virol. , vol.69 , pp. 2109-2114
    • Niedrig, M.1    Rabanus, J.P.2    L'Age Stehr, J.3    Gelderblom, H.R.4    Pauli, G.5
  • 24
    • 0023761449 scopus 로고
    • Development of a sensitive quantitative focal assay for human immunodeficiency virus infectivity
    • Chesebro B., and Wehrly K. Development of a sensitive quantitative focal assay for human immunodeficiency virus infectivity. J. Virol. 62 (1988) 3779-3788
    • (1988) J. Virol. , vol.62 , pp. 3779-3788
    • Chesebro, B.1    Wehrly, K.2
  • 25
    • 0002051756 scopus 로고
    • Quantitative assays for virus infectivity
    • Aldovini A., and Walker B. (Eds), Stockton Press, New York, NY
    • Johnson V.A., and Byington R.E. Quantitative assays for virus infectivity. In: Aldovini A., and Walker B. (Eds). Techniques of HIV Research (1990), Stockton Press, New York, NY 53-83
    • (1990) Techniques of HIV Research , pp. 53-83
    • Johnson, V.A.1    Byington, R.E.2
  • 26
    • 37849007571 scopus 로고    scopus 로고
    • Effects of partial deletions within the human immunodeficiency virus type 1 V3 loop on coreceptor tropism and sensitivity to entry inhibitors
    • Nolan K.M., Jordan A.P., and Hoxie J.A. Effects of partial deletions within the human immunodeficiency virus type 1 V3 loop on coreceptor tropism and sensitivity to entry inhibitors. J. Virol. 82 (2008) 664-673
    • (2008) J. Virol. , vol.82 , pp. 664-673
    • Nolan, K.M.1    Jordan, A.P.2    Hoxie, J.A.3
  • 28
    • 0029956382 scopus 로고    scopus 로고
    • Loss of antibody reactivity directed against the V3 domain of certain human immunodeficiency virus type 1 variants during disease progression
    • Schreiber M., Wachsmuth C., Müller H., Hagen C., Schmitz H., and van Lunzen J. Loss of antibody reactivity directed against the V3 domain of certain human immunodeficiency virus type 1 variants during disease progression. J. Gen. Virol. 77 (1996) 2403-2414
    • (1996) J. Gen. Virol. , vol.77 , pp. 2403-2414
    • Schreiber, M.1    Wachsmuth, C.2    Müller, H.3    Hagen, C.4    Schmitz, H.5    van Lunzen, J.6
  • 30
    • 0035918220 scopus 로고    scopus 로고
    • N-linked glycosylation of the HIV type-1 gp120 envelope glycoprotein as a major determinant of CCR5 and CXCR4 coreceptor utilization
    • Pollakis G., Kang S., Kliphuis A., Chalaby M.I., Goudsmit J., and Paxton W.A. N-linked glycosylation of the HIV type-1 gp120 envelope glycoprotein as a major determinant of CCR5 and CXCR4 coreceptor utilization. J. Biol. Chem. 276 (2001) 13433-13441
    • (2001) J. Biol. Chem. , vol.276 , pp. 13433-13441
    • Pollakis, G.1    Kang, S.2    Kliphuis, A.3    Chalaby, M.I.4    Goudsmit, J.5    Paxton, W.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.