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Volumn 26, Issue 1, 2002, Pages 42-49

Functional homologs of cyanovirin-N amenable to mass production in prokaryotic and eukaryotic hosts

Author keywords

Anti HIV; CV N; Cyanovirin N; Cyanovirins; HIV; Microbicides

Indexed keywords

BACTERIA (MICROORGANISMS); EUKARYOTA; HUMAN IMMUNODEFICIENCY VIRUS; PROKARYOTA;

EID: 0036417851     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(02)00513-2     Document Type: Article
Times cited : (46)

References (37)
  • 2
    • 0031559765 scopus 로고    scopus 로고
    • Isolation, primary sequence determination, and disulfide bond structure of cyanovirin-N, an anti-HIV (human immunodeficiency virus) protein from the cyanobacterium Nostoc ellipsosporum
    • K.R. Gustafson, R.C. Sowder II, L.E. Henderson, J.H. Cardellina II, J.B. McMahon, U. Rajamani, L.K. Pannell, M.R. Boyd, Isolation, primary sequence determination, and disulfide bond structure of cyanovirin-N, an anti-HIV (human immunodeficiency virus) protein from the cyanobacterium Nostoc ellipsosporum, Biochem. Biophys. Res. Commun. 238 (1) (1997) 223-228.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , Issue.1 , pp. 223-228
    • Gustafson, K.R.1    Sowder R.C. II2    Henderson, L.E.3    Cardellina J.H. II4    McMahon, J.B.5    Rajamani, U.6    Pannell, L.K.7    Boyd, M.R.8
  • 3
    • 0032030441 scopus 로고    scopus 로고
    • Recombinant production of cyano-virin-N, a potent human immunodeficiency virus-inactivating protein derived from a cultured cyanobacterium
    • T. Mori, K.R. Gustafson, L.K. Pannell, R.H. Shoemaker, L. Wu, J.B. McMahon, M.R. Boyd, Recombinant production of cyano-virin-N, a potent human immunodeficiency virus-inactivating protein derived from a cultured cyanobacterium, Protein Expr. Purif. 12 (2) (1998) 151-158.
    • (1998) Protein Expr. Purif. , vol.12 , Issue.2 , pp. 151-158
    • Mori, T.1    Gustafson, K.R.2    Pannell, L.K.3    Shoemaker, R.H.4    Wu, L.5    McMahon, J.B.6    Boyd, M.R.7
  • 5
    • 0033532212 scopus 로고    scopus 로고
    • Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping
    • F. Yang, C.A. Bewley, J.M. Louis, K.R. Gustafson, A.M. Gronenborn, G.M. Clore, A. Wlodower, Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping, J. Mol. Biol. 288 (3) (1999) 403-412.
    • (1999) J. Mol. Biol. , vol.288 , Issue.3 , pp. 403-412
    • Yang, F.1    Bewley, C.A.2    Louis, J.M.3    Gustafson, K.R.4    Gronenborn, A.M.5    Clore, G.M.6    Wlodower, A.7
  • 6
    • 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
    • B. Dey, D.L. Lerner, P. Lusso, M.R. Boyd, J.H. Elder, E.A. Berger, 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 (10) (2000) 4562-4569.
    • (2000) J. Virol. , 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
  • 8
    • 0032921247 scopus 로고    scopus 로고
    • Cyanovirin-N binds to gp120 to interfere with CD4-dependent human immunodeficiency virus type 1 virion binding, fusion, and infectivity but does not aNect the CD4 binding site on gp120 or soluble CD4-induced conformational changes in gp120
    • M.T. Esser, T. Mori, I. Mondor, Q. Sattentau, B. Dey, E.A. Berger, M.R. Boyd, J.D. Lifson, Cyanovirin-N binds to gp120 to interfere with CD4-dependent human immunodeficiency virus type 1 virion binding, fusion, and infectivity but does not aNect the CD4 binding site on gp120 or soluble CD4-induced conformational changes in gp120, J. Virol. 73 (5) (1999) 4360-4371.
    • (1999) J. Virol. , vol.73 , Issue.5 , pp. 4360-4371
    • Esser, M.T.1    Mori, T.2    Mondor, I.3    Sattentau, Q.4    Dey, B.5    Berger, E.A.6    Boyd, M.R.7    Lifson, J.D.8
  • 9
    • 0035112229 scopus 로고    scopus 로고
    • Cyanovirin-N, a potent human immunodeficiency virus-inactivating protein, blocks both CD4-dependent and CD4-independent binding of soluble gp120 (sgp120) to target cells, inhibits soluble CD4-induced binding of sgp120 to cell-associated CXCR4, and dissociates bound sgp120 from target cells
    • T. Mori, M.R. Boyd, Cyanovirin-N, a potent human immunode-ficiency virus-inactivating protein, blocks both CD4-dependent and CD4-independent binding of soluble gp120 (sgp120) to target cells, inhibits soluble CD4-induced binding of sgp120 to cell-associated CXCR4, and dissociates bound sgp120 from target cells, Antimicrob. Agents Chemother. 45 (3) (2001) 664-672.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , Issue.3 , pp. 664-672
    • Mori, T.1    Boyd, M.R.2
  • 10
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glyco-protein in complex with the CD4 receptor and a neutralizing human antibody
    • P.D. Kwong, R. Wyatt, J. Robinson, R.W. Sweets, J. Sodroski, W.A. Hendrickson, Structure of an HIV gp120 envelope glyco-protein in complex with the CD4 receptor and a neutralizing human antibody, Nature 393 (6686) (1998) 648-659.
    • (1998) Nature , vol.393 , Issue.6686 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweets, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 13
    • 0034640030 scopus 로고    scopus 로고
    • Microbicides: Ideas flourish, money to follow?
    • J. Stephenson, Microbicides: Ideas flourish, money to follow?, JAMA 283 (14) (2000) 1811-1812.
    • (2000) JAMA , vol.283 , Issue.14 , pp. 1811-1812
    • Stephenson, J.1
  • 14
    • 0033289665 scopus 로고    scopus 로고
    • Microbicides and barrier methods in HIV prevention
    • L. Van Damme, Z.F. Rosenberg, Microbicides and barrier methods in HIV prevention, AIDS 13 (Suppl. A) (1999) S85-S92.
    • (1999) AIDS , vol.13 , Issue.SUPPL. A
    • Van Damme, L.1    Rosenberg, Z.F.2
  • 15
    • 0343431526 scopus 로고    scopus 로고
    • Current evidence and future directions for targeting HIV entry: Therapeutic and prophylactic strategies
    • M.P. D'Souza, J.S. Cairns, S.F. Plaeger, Current evidence and future directions for targeting HIV entry: Therapeutic and prophylactic strategies, JAMA 284 (2) (2000) 215-222.
    • (2000) JAMA , vol.284 , Issue.2 , pp. 215-222
    • D'Souza, M.P.1    Cairns, J.S.2    Plaeger, S.F.3
  • 16
    • 0033667765 scopus 로고    scopus 로고
    • Molecular farming of pharmaceutical proteins
    • R. Fischer, N. Emans, Molecular farming of pharmaceutical proteins, Transgenic Res. 9 (4-5) (2000) 279-299.
    • (2000) Transgenic Res. , vol.9 , Issue.4-5 , pp. 279-299
    • Fischer, R.1    Emans, N.2
  • 18
    • 0033824414 scopus 로고    scopus 로고
    • Plants as bioreactors for protein production: Avoiding the problem of transgene silencing
    • C. De Wilde, H. Van Houdt, S. De Buck, G. Angenon, G. De Jaeger, A. Depicker, Plants as bioreactors for protein production: Avoiding the problem of transgene silencing, Plant Mol. Biol. 43 (2-3) (2000) 347-359.
    • (2000) Plant Mol. Biol. , vol.43 , Issue.2-3 , pp. 347-359
    • De Wilde, C.1    Van Houdt, H.2    De Buck, S.3    Angenon, G.4    De Jaeger, G.5    Depicker, A.6
  • 19
    • 0033672657 scopus 로고    scopus 로고
    • Transgenic animal bioreactors
    • L.M. Houdebine, Transgenic animal bioreactors, Transgenic Res. 9 (4-5) (2000) 305-320.
    • (2000) Transgenic Res. , vol.9 , Issue.4-5 , pp. 305-320
    • Houdebine, L.M.1
  • 20
    • 0033987460 scopus 로고    scopus 로고
    • Developing effcient strategies for the generation of transgenic cattle which produce biopharmaceuticals in milk
    • M.F. Brink, M.D. Bishop, F.R. Pieper, Developing effcient strategies for the generation of transgenic cattle which produce biopharmaceuticals in milk, Theriogenology 53 (1) (2000) 139-148.
    • (2000) Theriogenology , vol.53 , Issue.1 , pp. 139-148
    • Brink, M.F.1    Bishop, M.D.2    Pieper, F.R.3
  • 22
    • 0027257568 scopus 로고
    • Microwave miniprep of total genomic DNA from fungi, plants, protists and animals for PCR
    • D.C. Goodwin, S.B. Lee, Microwave miniprep of total genomic DNA from fungi, plants, protists and animals for PCR, Biotechniques 15 (3) (1993) 438-444.
    • (1993) Biotechniques , vol.15 , Issue.3 , pp. 438-444
    • Goodwin, D.C.1    Lee, S.B.2
  • 23
    • 0036113691 scopus 로고    scopus 로고
    • The domain-swapped dimer of cyanovirin-N is in a metastable folding intermediate. Reconciliation of X-ray and NMR structures
    • L.G. Barrientos, J.M. Louis, I. Botos, T. Mori, Z.Z. Han, B.R. O'Keefe, M.R. Boyd, A. Wlodawer, A.M. Gronenborn, The domain-swapped dimer of cyanovirin-N is in a metastable folding intermediate. Reconciliation of X-ray and NMR structures, Structure 10 (5) (2002) 673-686.
    • (2002) Structure , vol.10 , Issue.5 , pp. 673-686
    • Barrientos, L.G.1    Louis, J.M.2    Botos, I.3    Mori, T.4    Han, Z.Z.5    O'Keefe, B.R.6    Boyd, M.R.7    Wlodawer, A.8    Gronenborn, A.M.9
  • 24
    • 0002343673 scopus 로고
    • Measuring the conformational stability of a protein
    • T.E. Creighton (Ed.), IRL Press, Oxford, NY
    • C.N. Pace, B.A. Shirley, J.A. Thomson, Measuring the conformational stability of a protein, in: T.E. Creighton (Ed.), Protein Structure: A Practical Approach, IRL Press, Oxford, NY, 1989, pp. 311-329.
    • (1989) Protein Structure: A Practical Approach , pp. 311-329
    • Pace, C.N.1    Shirley, B.A.2    Thomson, J.A.3
  • 25
    • 0027967566 scopus 로고
    • Potent and specific inhibition of HIV envelope-mediated cell fusion and virus binding by G quartet-forming oligonucleotide (ISIS 5320)
    • R.W. Buckheit Jr., J.L. Roberson, C. Lackman-Smith, J.R. Wyatt, T.A. Vickers, D.J. Ecker, Potent and specific inhibition of HIV envelope-mediated cell fusion and virus binding by G quartet-forming oligonucleotide (ISIS 5320), AIDS Res. Hum. Retrovir. 10 (11) (1994) 1497-1506.
    • (1994) AIDS Res. Hum. Retrovir. , vol.10 , Issue.11 , pp. 1497-1506
    • Buckheit R.W., Jr.1    Roberson, J.L.2    Lackman-Smith, C.3    Wyatt, J.R.4    Vickers, T.A.5    Ecker, D.J.6
  • 29
    • 0024336222 scopus 로고
    • Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases
    • F. Maley, R.B. Trimble, A.L. Tarentino, T.H Plummer Jr., Characterization of glycoproteins and their associated oligosac-charides through the use of endoglycosidases, Anal. Biochem. 180 (2) (1989) 195-204.
    • (1989) Anal. Biochem. , vol.180 , Issue.2 , pp. 195-204
    • Maley, F.1    Trimble, R.B.2    Tarentino, A.L.3    Plummer T.H., Jr.4
  • 30
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • M.W. MacArthur, J.M. Thornton, Influence of proline residues on protein conformation, J. Mol. Biol. 218 (2) (1991) 397-412.
    • (1991) J. Mol. Biol. , vol.218 , Issue.2 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 31
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • M.W. Matthews, H. Nicholson, W.J. Becktel, Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding, Proc. Natl. Acad. Sci. USA 84 (19) (1987) 6663-6667.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , Issue.19 , pp. 6663-6667
    • Matthews, M.W.1    Nicholson, H.2    Becktel, W.J.3
  • 32
    • 0032168897 scopus 로고    scopus 로고
    • Compartment-specific accumulation of recombinant immunoglobulins in plant cells: An essential tool for antibody production and immunomodulation of physiological functions and pathogen activity
    • U. Conrad, U. Fiedler, Compartment-specific accumulation of recombinant immunoglobulins in plant cells: An essential tool for antibody production and immunomodulation of physiological functions and pathogen activity, Plant Mol. Biol. 38 (1/2) (1998) 101-109.
    • (1998) Plant Mol. Biol. , vol.38 , Issue.1-2 , pp. 101-109
    • Conrad, U.1    Fiedler, U.2
  • 36
    • 0032727666 scopus 로고    scopus 로고
    • A Review of oral vaccination with transgenic vegetables
    • C.O. Tacket, H.S. Mason, A review of oral vaccination with transgenic vegetables, Microbes Infect. 1 (10) (1999) 777-783.
    • (1999) Microbes Infect. , vol.1 , Issue.10 , pp. 777-783
    • Tacket, C.O.1    Mason, H.S.2
  • 37
    • 0031863854 scopus 로고    scopus 로고
    • Immunogenicity in humans of a recombinant bacterial antigen delivered in a transgenic potato
    • C.O. Tacket, H.S. Mason, G. Losonsky, J.D. Clements, M.M. Levine, C.J. Arntzen, Immunogenicity in humans of a recombinant bacterial antigen delivered in a transgenic potato, Nat. Med. 4 (5) (1998) 607-609.
    • (1998) Nat. Med. , vol.4 , Issue.5 , pp. 607-609
    • Tacket, C.O.1    Mason, H.S.2    Losonsky, G.3    Clements, J.D.4    Levine, M.M.5    Arntzen, C.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.