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Volumn 108, Issue 34, 2011, Pages 14079-14084

Designed oligomers of cyanovirin-N show enhanced HIV neutralization

Author keywords

Crystal structure; Domain swapped dimer; Protein engineering

Indexed keywords

CARBOHYDRATE; CYANOVIRIN N; DIMER; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; MONOMER; NEUTRALIZING ANTIBODY; OLIGOMER; TETRAMER;

EID: 80052169440     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1108777108     Document Type: Article
Times cited : (40)

References (44)
  • 2
    • 0033997468 scopus 로고    scopus 로고
    • Multiple antiviral activities of cyanovirin-N: Blocking of human immunodeficiency virus type 1 gp120 interaction with CD4 and coreceptor and inhibition of diverse enveloped viruses
    • DOI 10.1128/JVI.74.10.4562-4569.2000
    • Dey B, et al. (2000) Multiple antiviral activities of cyanovirin-N: blocking of human immunodeficiency virus type 1 gp120 interaction with CD4 and coreceptor and inhibition of diverse enveloped viruses. J Virol 74:4562-4569. (Pubitemid 30237881)
    • (2000) Journal of Virology , vol.74 , Issue.10 , pp. 4562-4569
    • Dey, B.1    Lerner, D.L.2    Lusso, P.3    Boyd, M.R.4    Elder, J.H.5    Berger, E.A.6
  • 5
    • 12344293665 scopus 로고    scopus 로고
    • The highly specific carbohydrate-binding protein cyanovirin-N: Structure, anti-HIV/Ebola activity and possibilities for therapy
    • Barrientos LG, Gronenborn AM (2005) The highly specific carbohydrate-binding protein cyanovirin-N: structure, anti-HIV/Ebola activity and possibilities for therapy. Mini-Rev Med Chem 5:21-31. (Pubitemid 40124840)
    • (2005) Mini-Reviews in Medicinal Chemistry , vol.5 , Issue.1 , pp. 21-31
    • Barrientos, L.G.1    Gronenborn, A.M.2
  • 6
    • 0242586063 scopus 로고    scopus 로고
    • Cyanovirin-N binds to the viral surface glycoprotein, GP1,2 and inhibits infectivity of Ebola virus
    • Barrientos LG, et al. (2003) Cyanovirin-N binds to the viral surface glycoprotein, GP1,2 and inhibits infectivity of Ebola virus. Antiviral Res 58:47-56.
    • (2003) Antiviral Res , vol.58 , pp. 47-56
    • Barrientos, L.G.1
  • 9
    • 0034799906 scopus 로고    scopus 로고
    • The potent anti-HIV protein cyanovirin-N contains two novel carbohydrate binding sites that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinity: Implications for binding to the HIV envelope protein gp120
    • Bewley CA, Otero-Quintero S (2001) The potent anti-HIV protein cyanovirin-N contains two novel carbohydrate binding sites that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinity: implications for binding to the HIV envelope protein gp120. J Am Chem Soc 123:3892-3902.
    • (2001) J Am Chem Soc 123 , pp. 3892-3902
    • Bewley, C.A.1    Otero-Quintero, S.2
  • 11
    • 0035028207 scopus 로고    scopus 로고
    • Cyanovirin-N defines a new class of antiviral agent targeting N-linked, high-mannose glycans in an oligosaccharide-specific manner
    • Bolmstedt AJ, O'Keefe BR, Shenoy SR, McMahon JB, Boyd MR (2001) Cyanovirin-N defines a new class of antiviral agent targeting N-linked, high-mannose glycans in an oligosaccharide-specific manner. Mol Pharmacol 59:949-954. (Pubitemid 32381571)
    • (2001) Molecular Pharmacology , vol.59 , Issue.5 , pp. 949-954
    • Bolmstedt, A.J.1    O'Keefe, B.R.2    Shenoy, S.R.3    Mcmahon, J.B.4    Boyd, M.R.5
  • 13
    • 0035040784 scopus 로고    scopus 로고
    • Selective interactions of the human immunodeficiency virus-inactivating protein cyanovirin-N with high-mannose oligosaccharides on gp120 and other glycoproteins
    • Shenoy SR, O'Keefe BR, Bolmstedt AJ, Cartner LK, Boyd MR (2001) Selective interactions of the human immunodeficiency virus-inactivating protein cyanovirin-N with high-mannose oligosaccharides on gp120 and other glycoproteins. J Pharmacol Exp Ther 297:704-710. (Pubitemid 32378003)
    • (2001) Journal of Pharmacology and Experimental Therapeutics , vol.297 , Issue.2 , pp. 704-710
    • Shenoy, S.R.1    O'Keefe, B.R.2    Bolmstedt, A.J.3    Cartner, L.K.4    Boyd, M.R.5
  • 15
    • 0037072880 scopus 로고    scopus 로고
    • Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharides
    • Botos I, et al. (2002) Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharides. J Biol Chem 277:34336-34342.
    • (2002) J Biol Chem , vol.277 , pp. 34336-34342
    • Botos, I.1
  • 16
    • 33845632976 scopus 로고    scopus 로고
    • Dissecting carbohydrate-Cyanovirin-N binding by structure-guided mutagenesis: Functional implications for viral entry inhibition
    • DOI 10.1093/protein/gzl040
    • Barrientos LG, Matei E, Lasala F, Delgado R, Gronenborn AM (2006) Dissecting carbohydrate- Cyanovirin-N binding by structure-guided mutagenesis: functional implications for viral entry inhibition. Protein Eng Des Sel 19:525-535. (Pubitemid 44950458)
    • (2006) Protein Engineering, Design and Selection , vol.19 , Issue.12 , pp. 525-535
    • Barrientos, L.G.1    Matei, E.2    Lasala, F.3    Delgado, R.4    Gronenborn, A.M.5
  • 17
    • 34547916495 scopus 로고    scopus 로고
    • A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity
    • DOI 10.1021/bi700666m
    • Fromme R, et al. (2007) A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity. Biochemistry 46:9199-9207. (Pubitemid 47255034)
    • (2007) Biochemistry , vol.46 , Issue.32 , pp. 9199-9207
    • Fromme, R.1    Katiliene, Z.2    Giomarelli, B.3    Bogani, F.4    Mc, M.J.5    Mori, T.6    Fromme, P.7    Ghirlanda, G.8
  • 18
    • 67549112686 scopus 로고    scopus 로고
    • Multivalent interactions with gp120 are required for the anti-HIV activity of Cyanovirin
    • Liu Y, et al. (2009) Multivalent interactions with gp120 are required for the anti-HIV activity of Cyanovirin. Biopolymers 92:194-200.
    • (2009) Biopolymers , vol.92 , pp. 194-200
    • Liu, Y.1
  • 19
    • 77951219869 scopus 로고    scopus 로고
    • Anti-HIV activity of defective cyanovirin-N mutants is restored by dimerization
    • Matei E, et al. (2010) Anti-HIV activity of defective cyanovirin-N mutants is restored by dimerization. J Biol Chem 285:13057-13065.
    • (2010) J Biol Chem , vol.285 , pp. 13057-13065
    • Matei, E.1
  • 20
    • 4644253146 scopus 로고    scopus 로고
    • Flipping the switch from monomeric to dimeric CV-N has little effect on antiviral activity
    • DOI 10.1016/j.str.2004.07.019, PII S0969212604002886
    • Barrientos LG, Lasala F, Delgado R, Sanchez A, Gronenborn AM (2004) Flipping the switch from monomeric to dimeric CV-N has little effect on antiviral activity. Structure 12:1799-1807. (Pubitemid 39298964)
    • (2004) Structure , vol.12 , Issue.10 , pp. 1799-1807
    • Barrientos, L.G.1    Lasala, F.2    Delgado, R.3    Sanchez, A.4    Gronenborn, A.M.5
  • 21
    • 0037012366 scopus 로고    scopus 로고
    • Engineering an obligate domain-swapped dimer of cyanovirin-n with enhanced anti-hiv activity
    • DOI 10.1021/ja025537m
    • Kelley BS, Chang LC, Bewley CA (2002) Engineering an obligate domain-swapped dimer of cyanovirin-N with enhanced anti-HIV activity. J Am Chem Soc 124:3210-3211. (Pubitemid 34270352)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.13 , pp. 3210-3211
    • Kelley, B.S.1    Leng, C.C.2    Bewley, C.A.3
  • 28
    • 0028593629 scopus 로고
    • A broadly neutralizing human monoclonal antibody against gp41 of human immunodeficiency virus type 1
    • Purtscher M, et al. (1994) A broadly neutralizing human monoclonal antibody against gp41 of human immunodeficiency virus type 1. AIDS Res Hum Retroviruses 10:1651-1658.
    • (1994) AIDS Res Hum Retroviruses , vol.10 , pp. 1651-1658
    • Purtscher, M.1
  • 30
    • 70349887757 scopus 로고    scopus 로고
    • Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target
    • Walker LM, et al. (2009) Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target. Science 326:285-289.
    • (2009) Science , vol.326 , pp. 285-289
    • Walker, L.M.1
  • 31
    • 77954920017 scopus 로고    scopus 로고
    • Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1
    • Wu X, et al. (2010) Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1. Science 329:856-861.
    • (2010) Science , vol.329 , pp. 856-861
    • Wu, X.1
  • 33
    • 72849116535 scopus 로고    scopus 로고
    • Evaluation of CD4-CD4i antibody architectures yields potent, broadly cross-reactive anti-human immunodeficiency virus reagents
    • West AP, Jr, et al. (2010) Evaluation of CD4-CD4i antibody architectures yields potent, broadly cross-reactive anti-human immunodeficiency virus reagents. J Virol 84:261-269.
    • (2010) J Virol , vol.84 , pp. 261-269
    • West Jr., A.P.1
  • 34
    • 0036307699 scopus 로고    scopus 로고
    • Potent inhibition of HIV-1 fusion by cyanovirin-N requires only a single high affinity carbohydrate binding site: Characterization of low affinity carbohydrate binding site knockout mutants
    • DOI 10.1016/S0022-2836(02)00045-1
    • Chang LC, Bewley CA (2002) Potent inhibition of HIV-1 fusion by cyanovirin-N requires only a single high affinity carbohydrate binding site: characterization of low affinity carbohydrate binding site knockout mutants. J Mol Biol 318:1-8. (Pubitemid 34729380)
    • (2002) Journal of Molecular Biology , vol.318 , Issue.1 , pp. 1-8
    • Chang, L.C.1    Bewley, C.A.2
  • 37
    • 51449112802 scopus 로고    scopus 로고
    • A review of current intravaginal drug delivery approaches employed for the prophylaxis of HIV/AIDS and prevention of sexually transmitted infections
    • Ndesendo VM, et al. (2008) A review of current intravaginal drug delivery approaches employed for the prophylaxis of HIV/AIDS and prevention of sexually transmitted infections. AAPS PharmSciTech 9:505-520.
    • (2008) AAPS PharmSciTech , vol.9 , pp. 505-520
    • Ndesendo, V.M.1
  • 38
    • 34247530859 scopus 로고    scopus 로고
    • Virus glycosylation: role in virulence and immune interactions
    • DOI 10.1016/j.tim.2007.03.003, PII S0966842X07000467
    • Vigerust DJ, Shepherd VL (2007) Virus glycosylation: role in virulence and immune interactions. Trends Microbiol 15:211-218. (Pubitemid 46660602)
    • (2007) Trends in Microbiology , vol.15 , Issue.5 , pp. 211-218
    • Vigerust, D.J.1    Shepherd, V.L.2
  • 39
    • 0025331559 scopus 로고
    • Role of N-linked glycans of envelope glycoproteins in infectivity of human immunodeficiency virus type 1
    • Fenouillet E, Gluckman JC, Bahraoui E (1990) Role of N-linked glycans of envelope glycoproteins in infectivity of human immunodeficiency virus type 1. J Virol 64:2841-2848. (Pubitemid 20171274)
    • (1990) Journal of Virology , vol.64 , Issue.6 , pp. 2841-2848
    • Fenouillet, E.1    Gluckman, J.C.2    Bahraoui, E.3
  • 41
    • 0028784138 scopus 로고
    • Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides
    • Stemmer WP, Crameri A, Ha KD, Brennan TM, Heyneker HL (1995) Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides. Gene 164:49-53.
    • (1995) Gene , vol.164 , pp. 49-53
    • Stemmer, W.P.1    Crameri, A.2    Ha, K.D.3    Brennan, T.M.4    Heyneker, H.L.5
  • 43
    • 0037456827 scopus 로고    scopus 로고
    • Antibody neutralization and escape by HIV-1
    • Wei XP, et al. (2003) Antibody neutralization and escape by HIV-1. Nature 422:307-312.
    • (2003) Nature , vol.422 , pp. 307-312
    • Wei, X.P.1
  • 44
    • 0034791996 scopus 로고    scopus 로고
    • Solution structure of a cyanovirin-N:Manα1-2Manα complex: Structural basis for high-affinity carbohydrate-mediated binding to gp120
    • Bewley CA (2001) Solution structure of a cyanovirin-N:Manα1- 2Manα complex: structural basis for high-affinity carbohydrate-mediated binding to gp120. Structure 9:931-940.
    • (2001) Structure , vol.9 , pp. 931-940
    • Bewley, C.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.