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Volumn 47, Issue 12, 2008, Pages 3625-3635

Atomic mapping of the sugar interactions in one-site and two-site mutants of cyanovirin-N by NMR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC MAPPING; PROTEIN BINDING SITE; TRIMANNOSIDES;

EID: 41149114081     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702200m     Document Type: Article
Times cited : (14)

References (36)
  • 1
    • 0030790094 scopus 로고    scopus 로고
    • Boyd, M. R., Gustafson, K. R., McMahon, J. B., Shoemaker, R. H., Okeefe, B. R., Mori, T., Gulakowski, R. J., Wu, L., Rivera, M. I., Laurencot, C. M., Currens, M. J., Cardellina, J. H., Buckheit, R. W., Nara, P. L., Pannell, L. K., Sowder, R. C., and Henderson, L. E. (1997) Discovery of Cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: Potential applications to microbicide development. Antimicrob. Agents Chemother. 41, 1521-1530.
    • Boyd, M. R., Gustafson, K. R., McMahon, J. B., Shoemaker, R. H., Okeefe, B. R., Mori, T., Gulakowski, R. J., Wu, L., Rivera, M. I., Laurencot, C. M., Currens, M. J., Cardellina, J. H., Buckheit, R. W., Nara, P. L., Pannell, L. K., Sowder, R. C., and Henderson, L. E. (1997) Discovery of Cyanovirin-N, a novel human immunodeficiency virus-inactivating protein that binds viral surface envelope glycoprotein gp120: Potential applications to microbicide development. Antimicrob. Agents Chemother. 41, 1521-1530.
  • 2
    • 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 affect the CD4 binding site on gp120 or soluble CD4-induced conformational changes in gp120
    • Esser, M. T., Mori, T., Mondor, I., Sattentau, Q. J., Dey, B., Berger, E. A., Boyd, M. R., and Lifson, J. D. (1999) Cyanovirin-N binds to gp120 to interfere with CD4-dependent human immunodeficiency virus type 1 virion binding, fusion, and infectivity but does not affect the CD4 binding site on gp120 or soluble CD4-induced conformational changes in gp120. J. Virol. 73, 4360-4371.
    • (1999) J. Virol , vol.73 , pp. 4360-4371
    • Esser, M.T.1    Mori, T.2    Mondor, I.3    Sattentau, Q.J.4    Dey, B.5    Berger, E.A.6    Boyd, M.R.7    Lifson, J.D.8
  • 3
    • 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
    • Dey, B., Lerner, D. L., Lusso, P., Boyd, M. R., Elder, J. H., and Berger, E. A. (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.
    • (2000) J. Virol , vol.74 , 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
  • 6
    • 12344293665 scopus 로고    scopus 로고
    • The highly specific carbohydrate-binding protein Cyanovirin-N: Structure, anti-HIV/Ebola activity and possibilities for therapy
    • Barrientos, L. G., and Gronenborn, A. M. (2005) The highly specific carbohydrate-binding protein Cyanovirin-N: Structure, anti-HIV/Ebola activity and possibilities for therapy. Rev. Med. Chem. 5, 21-31.
    • (2005) Rev. Med. Chem , vol.5 , pp. 21-31
    • Barrientos, L.G.1    Gronenborn, A.M.2
  • 7
    • 0033789322 scopus 로고    scopus 로고
    • Analysis of the interaction between the HIV-inactivating protein Cyanovirin-N and soluble forms of the envelope glycoproteins gp120 and gp41
    • O'Keefe, B. R., Shenoy, S. R., Xie, D., Zhang, W. T., Muschik, J. M., Currens, M. J., Chaiken, I., and Boyd, M. R. (2000) Analysis of the interaction between the HIV-inactivating protein Cyanovirin-N and soluble forms of the envelope glycoproteins gp120 and gp41. Mol. Pharmacol. 58, 982-992.
    • (2000) Mol. Pharmacol , vol.58 , pp. 982-992
    • O'Keefe, B.R.1    Shenoy, S.R.2    Xie, D.3    Zhang, W.T.4    Muschik, J.M.5    Currens, M.J.6    Chaiken, I.7    Boyd, M.R.8
  • 8
    • 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, A. J., O'Keefe, B. R., Shenoy, S. R., McMahon, J. B., and Boyd, M. R. (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.
    • (2001) Mol. Pharmacol , vol.59 , pp. 949-954
    • Bolmstedt, A.J.1    O'Keefe, B.R.2    Shenoy, S.R.3    McMahon, J.B.4    Boyd, M.R.5
  • 9
    • 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, S. R., O'Keefe, B. R., Bolmstedt, A. J., Cartner, L. K., and Boyd, M. R. (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.
    • (2001) J. Pharmacol. Exp. Ther , vol.297 , pp. 704-710
    • Shenoy, S.R.1    O'Keefe, B.R.2    Bolmstedt, A.J.3    Cartner, L.K.4    Boyd, M.R.5
  • 12
    • 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, C. A. (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
  • 15
    • 0037258662 scopus 로고    scopus 로고
    • Solution structure of a circular-permuted variant of the potent HIV-inactivating protein CyanovirinN: Structural basis for protein stability and oligosaccharide interaction
    • Barrientos, L. G., Louis, J. M., Ratner, D. M., Seeberger, P. H., and Gronenborn, A. M. (2003) Solution structure of a circular-permuted variant of the potent HIV-inactivating protein CyanovirinN: Structural basis for protein stability and oligosaccharide interaction. J. Mol. Biol. 325, 211-223.
    • (2003) J. Mol. Biol , vol.325 , pp. 211-223
    • Barrientos, L.G.1    Louis, J.M.2    Ratner, D.M.3    Seeberger, P.H.4    Gronenborn, A.M.5
  • 16
    • 0034799906 scopus 로고    scopus 로고
    • 9 with nanomolar affinity: Implications for binding to the HIV envelope protein gp120
    • 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 , vol.123 , pp. 3892-3902
    • Bewley, C.A.1    Otero-Quintero, S.2
  • 17
    • 0036773694 scopus 로고    scopus 로고
    • Multisite and multivalent binding between Cyanovirin-N and branched oligomannosides: Calorimetric and NMR characterization
    • Shenoy, S. R., Barrientos, L. G., Ratner, D. M., O'Keefe, B. R., Seeberger, P. H., Gronenborn, A. M., and Boyd, M. R. (2002) Multisite and multivalent binding between Cyanovirin-N and branched oligomannosides: Calorimetric and NMR characterization. Chem. Biol. 9, 1109-1118.
    • (2002) Chem. Biol , vol.9 , pp. 1109-1118
    • Shenoy, S.R.1    Barrientos, L.G.2    Ratner, D.M.3    O'Keefe, B.R.4    Seeberger, P.H.5    Gronenborn, A.M.6    Boyd, M.R.7
  • 19
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • Mayer, M., and Meyer, B. (1999) Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew. Chem., Int. Ed. 38, 1784-1788.
    • (1999) Angew. Chem., Int. Ed , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 20
    • 0033538283 scopus 로고    scopus 로고
    • Detecting binding affinity to immobilized receptor proteins in compound libraries by HR-MAS STD NMR
    • Klein, J., Meinecke, R., Mayer, M., and Meyer, B. (1999) Detecting binding affinity to immobilized receptor proteins in compound libraries by HR-MAS STD NMR. J. Am. Chem. Soc. 121, 5336-5337.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 5336-5337
    • Klein, J.1    Meinecke, R.2    Mayer, M.3    Meyer, B.4
  • 21
    • 0034725387 scopus 로고    scopus 로고
    • Application of NMR based binding assays to identify key hydroxy groups for intermolecular recognition
    • Vogtherr, M., and Peters, T. (2000) Application of NMR based binding assays to identify key hydroxy groups for intermolecular recognition. J. Am. Chem. Soc. 122, 6093-6099.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 6093-6099
    • Vogtherr, M.1    Peters, T.2
  • 22
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • Mayer, M., and Meyer, B. (2001) Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J. Am. Chem. Soc. 123, 6108-6117.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 23
    • 0037463033 scopus 로고    scopus 로고
    • NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors
    • Meyer, B., and Peters, T. (2003) NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors. Angew. Chem., Int. Ed. 42, 864-890.
    • (2003) Angew. Chem., Int. Ed , vol.42 , pp. 864-890
    • Meyer, B.1    Peters, T.2
  • 24
    • 8344235090 scopus 로고    scopus 로고
    • Atomic mapping of the interactions between the antiviral agent Cyanovirin-N and oligomannosides by saturation-transfer difference NMR
    • Sandström, C., Berteau, O., Gemma, E., Oscarson, S., Kenne, L., and Gronenborn, A. M. (2004) Atomic mapping of the interactions between the antiviral agent Cyanovirin-N and oligomannosides by saturation-transfer difference NMR. Biochemistry 43, 13926-13931.
    • (2004) Biochemistry , vol.43 , pp. 13926-13931
    • Sandström, C.1    Berteau, O.2    Gemma, E.3    Oscarson, S.4    Kenne, L.5    Gronenborn, A.M.6
  • 25
    • 33845632976 scopus 로고    scopus 로고
    • Dissecting carbohydrate-Cyanovirin-N binding by structure-guided mutagenesis: Functional implications for viral entry inhibition
    • Barrientos, L. G., Matei, E., Lasala, F., Delgado, R., and Gronenborn, A. M. (2006) Dissecting carbohydrate-Cyanovirin-N binding by structure-guided mutagenesis: Functional implications for viral entry inhibition. Protein Eng., Des. Sel. 19, 525-535.
    • (2006) Protein Eng., Des. Sel , vol.19 , pp. 525-535
    • Barrientos, L.G.1    Matei, E.2    Lasala, F.3    Delgado, R.4    Gronenborn, A.M.5
  • 26
    • 10944256235 scopus 로고    scopus 로고
    • Competition STD NMR for the detection of high-affinity ligands and NMR-based screening
    • Wang, Y. S., Liu, D. J., and Wyss, D. F. (2004) Competition STD NMR for the detection of high-affinity ligands and NMR-based screening. Magn. Reson. Chem. 42, 485-489.
    • (2004) Magn. Reson. Chem , vol.42 , pp. 485-489
    • Wang, Y.S.1    Liu, D.J.2    Wyss, D.F.3
  • 27
    • 0028892457 scopus 로고
    • Synthesis of deoxy analogues of methyl 3,6-di-O-α-D-mannopyranosyl-α-D- mannopyranoside for studies of the binding site of Concanavalin A
    • Oscarson, S., and Tedebark, U. (1995) Synthesis of deoxy analogues of methyl 3,6-di-O-α-D-mannopyranosyl-α-D- mannopyranoside for studies of the binding site of Concanavalin A. Carbohydr. Res. 278, 271-287.
    • (1995) Carbohydr. Res , vol.278 , pp. 271-287
    • Oscarson, S.1    Tedebark, U.2
  • 28
    • 33646919630 scopus 로고    scopus 로고
    • Synthesis of monodeoxy analogues of the trisaccharide α-D-Glcp-(1-3)-α-D- Manp-(1-2)-α-D-ManpOMe recognized by calreticuli/calnexin
    • Gemma, E., Lahmann, M., and Oscarson, S. (2006) Synthesis of monodeoxy analogues of the trisaccharide α-D-Glcp-(1-3)-α-D- Manp-(1-2)-α-D-ManpOMe recognized by calreticuli/calnexin. Carbohydr. Res. 341, 1533-1542.
    • (2006) Carbohydr. Res , vol.341 , pp. 1533-1542
    • Gemma, E.1    Lahmann, M.2    Oscarson, S.3
  • 29
    • 0028109186 scopus 로고    scopus 로고
    • Boger, D. L., and Honda, T. (1994) Total synthesis of Bleomycin A2 and related agents. 4. Synthesis of the disaccharide subunit 2-O-(3O-carbamoyl-α-D-mannopyrannosyl)-L-gulopyranose and completion of the total synthesis of bleomycin A2. J. Am. Chem. Soc. 116, 5647-5656.
    • Boger, D. L., and Honda, T. (1994) Total synthesis of Bleomycin A2 and related agents. 4. Synthesis of the disaccharide subunit 2-O-(3O-carbamoyl-α-D-mannopyrannosyl)-L-gulopyranose and completion of the total synthesis of bleomycin A2. J. Am. Chem. Soc. 116, 5647-5656.
  • 30
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 31
    • 0043032424 scopus 로고    scopus 로고
    • The effect of relaxation on the epitope mapping by saturation transfer difference NMR
    • Yan, J. L., Kline, A. D., Mo, H. P., Shapiro, M. J., and Zartler, E. R. (2003) The effect of relaxation on the epitope mapping by saturation transfer difference NMR. J. Magn. Reson. 163, 270-276.
    • (2003) J. Magn. Reson , vol.163 , pp. 270-276
    • Yan, J.L.1    Kline, A.D.2    Mo, H.P.3    Shapiro, M.J.4    Zartler, E.R.5
  • 32
    • 0037176251 scopus 로고    scopus 로고
    • Saturation transfer difference 1D-TOCSY experiments to map the topography of oligosaccharides recognized by a monoclonal antibody directed against the cell-wall polysaccharide of group A Streptococcus
    • Johnson, M. A., and Pinto, B. M. (2002) Saturation transfer difference 1D-TOCSY experiments to map the topography of oligosaccharides recognized by a monoclonal antibody directed against the cell-wall polysaccharide of group A Streptococcus. J. Am. Chem. Soc. 124, 15368-15374.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 15368-15374
    • Johnson, M.A.1    Pinto, B.M.2
  • 33
    • 1842450536 scopus 로고    scopus 로고
    • NMR-based characterization of phenothiazines as a RNA binding scaffold
    • Meyer, M., and James, T. L. (2004) NMR-based characterization of phenothiazines as a RNA binding scaffold. J. Am. Chem. Soc. 126, 4453-4460.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 4453-4460
    • Meyer, M.1    James, T.L.2
  • 35
    • 0346786324 scopus 로고    scopus 로고
    • Saturation transfer difference NMR and computational modeling of a sialoadhesin-sialyl lactose complex
    • Bhunia, A., Jayalakshmi, V., Benie, A. J., Schuster, O., Kelm, S., Krishna, N. R., and Peters, T. (2004) Saturation transfer difference NMR and computational modeling of a sialoadhesin-sialyl lactose complex. Carbohydr. Res. 339, 259-267.
    • (2004) Carbohydr. Res , vol.339 , pp. 259-267
    • Bhunia, A.1    Jayalakshmi, V.2    Benie, A.J.3    Schuster, O.4    Kelm, S.5    Krishna, N.R.6    Peters, T.7
  • 36
    • 36849104960 scopus 로고
    • Measurement of spin relaxation in complex systems
    • Vold, R. L., Waugh, J. S., Klein, M. P., and Phelps, D. E. (1968) Measurement of spin relaxation in complex systems. J. Chem. Phys. 48, 3831.
    • (1968) J. Chem. Phys , vol.48 , pp. 3831
    • Vold, R.L.1    Waugh, J.S.2    Klein, M.P.3    Phelps, D.E.4


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