메뉴 건너뛰기




Volumn 393, Issue 1, 2009, Pages 112-119

Affinity maturation by targeted diversification of the CDR-H2 loop of a monoclonal Fab derived from a synthetic naïve human antibody library and directed against the internal trimeric coiled-coil of gp41 yields a set of Fabs with improved HIV-1 neutralization potency and breadth

Author keywords

Affinity maturation; Broadly neutralizing antibodies; gp41 envelope; HIV 1; Naive phage library

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN; VIRUS GLYCOPROTEIN 41;

EID: 70349380779     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2009.07.019     Document Type: Article
Times cited : (21)

References (57)
  • 1
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease
    • Berger E.A., Murphy P.M., and Farber J.M. Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease. Annu. Rev. Immunol. 17 (1999) 657-700
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 2
    • 0037134497 scopus 로고    scopus 로고
    • Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41
    • Bewley C.A., Louis J.M., Ghirlando R., and Clore G.M. Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41. J. Biol. Chem. 277 (2002) 14238-14245
    • (2002) J. Biol. Chem. , vol.277 , pp. 14238-14245
    • Bewley, C.A.1    Louis, J.M.2    Ghirlando, R.3    Clore, G.M.4
  • 4
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan D.C., and Kim P.S. HIV entry and its inhibition. Cell 93 (1998) 681-684
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 5
    • 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
  • 6
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
    • Chan D.C., Chutkowski C.T., and Kim P.S. Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 15613-15617
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 7
    • 0034634920 scopus 로고    scopus 로고
    • Monoclonal antibodies that bind to the core of fusion-active glycoprotein 41. AIDS Res
    • Chen C.H., Greenberg M.L., Bolognesi D.P., and Matthews T.J. Monoclonal antibodies that bind to the core of fusion-active glycoprotein 41. AIDS Res. Hum. Retroviruses 16 (2000) 2037-2041
    • (2000) Hum. Retroviruses , vol.16 , pp. 2037-2041
    • Chen, C.H.1    Greenberg, M.L.2    Bolognesi, D.P.3    Matthews, T.J.4
  • 9
    • 0019882480 scopus 로고
    • Generalized equations for the analysis of inhibitions of Michaelis-Menten and higher-order kinetic systems with two or more mutually exclusive and nonexclusive inhibitors
    • Chou T.C., and Talalay P. Generalized equations for the analysis of inhibitions of Michaelis-Menten and higher-order kinetic systems with two or more mutually exclusive and nonexclusive inhibitors. Eur. J. Biochem. 115 (1981) 207-216
    • (1981) Eur. J. Biochem. , vol.115 , pp. 207-216
    • Chou, T.C.1    Talalay, P.2
  • 10
    • 0021118703 scopus 로고
    • Quantitative analysis of dose-effect relationships: the combined effects of multiple drugs or enzyme inhibitors
    • Chou T.C., and Talalay P. Quantitative analysis of dose-effect relationships: the combined effects of multiple drugs or enzyme inhibitors. Adv. Enz. Regul. 22 (1984) 27-55
    • (1984) Adv. Enz. Regul. , vol.22 , pp. 27-55
    • Chou, T.C.1    Talalay, P.2
  • 11
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert D.M., and Kim P.S. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70 (2001) 777-810
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 12
    • 0035949493 scopus 로고    scopus 로고
    • Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
    • Eckert D.M., and Kim P.S. Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 11187-11192
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11187-11192
    • Eckert, D.M.1    Kim, P.S.2
  • 13
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket
    • Eckert D.M., Malashkevich V.N., Hong L.H., Carr P.A., and Kim P.S. Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell 99 (1999) 103-115
    • (1999) Cell , vol.99 , pp. 103-115
    • Eckert, D.M.1    Malashkevich, V.N.2    Hong, L.H.3    Carr, P.A.4    Kim, P.S.5
  • 14
    • 56749185286 scopus 로고    scopus 로고
    • Characterization of the steric defense of the HIV-1 gp41 N-trimer region
    • Eckert D.M., Shi Y., Kim S., Welch B.D., Kang E., Poff E.S., and Kay M.S. Characterization of the steric defense of the HIV-1 gp41 N-trimer region. Protein Sci. 17 (2008) 2091-2100
    • (2008) Protein Sci. , vol.17 , pp. 2091-2100
    • Eckert, D.M.1    Shi, Y.2    Kim, S.3    Welch, B.D.4    Kang, E.5    Poff, E.S.6    Kay, M.S.7
  • 15
    • 0024435050 scopus 로고
    • Mutational analysis of the cleavage sequence of the human immunodeficiency virus type 1 envelope glycoprotein precursor gp160
    • Freed E.O., Myers D.J., and Risser R. Mutational analysis of the cleavage sequence of the human immunodeficiency virus type 1 envelope glycoprotein precursor gp160. J. Virol. 63 (1989) 4670-4675
    • (1989) J. Virol. , vol.63 , pp. 4670-4675
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 16
    • 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. Nature Struct. Biol. 5 (1998) 276-279
    • (1998) Nature Struct. Biol. , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 19
    • 33750813866 scopus 로고    scopus 로고
    • Synergistic inhibition of HIV-1 envelope-mediated membrane fusion by inhibitors targeting the N and C-terminal heptad repeats of gp41
    • Gustchina E., Louis J.M., Bewley C.A., and Clore G.M. Synergistic inhibition of HIV-1 envelope-mediated membrane fusion by inhibitors targeting the N and C-terminal heptad repeats of gp41. J. Mol. Biol. 364 (2006) 283-289
    • (2006) J. Mol. Biol. , vol.364 , pp. 283-289
    • Gustchina, E.1    Louis, J.M.2    Bewley, C.A.3    Clore, G.M.4
  • 20
    • 36348931103 scopus 로고    scopus 로고
    • A monoclonal Fab derived from a human non-immune phage library reveals a new epitope on gp41 and neutralizes diverse HIV-1 strains
    • Gustchina E., Louis J.M., Lam S.N., Bewley C.A., and Clore G.M. A monoclonal Fab derived from a human non-immune phage library reveals a new epitope on gp41 and neutralizes diverse HIV-1 strains. J. Virol. 81 (2007) 12946-12953
    • (2007) J. Virol. , vol.81 , pp. 12946-12953
    • Gustchina, E.1    Louis, J.M.2    Lam, S.N.3    Bewley, C.A.4    Clore, G.M.5
  • 21
    • 53749101563 scopus 로고    scopus 로고
    • Mut(e,g) potentiates the human immunodeficiency virus type 1 neutralizing activity of monoclonal antibodies directed against the N-terminal helical repeat of gp41
    • Mut(e,g) potentiates the human immunodeficiency virus type 1 neutralizing activity of monoclonal antibodies directed against the N-terminal helical repeat of gp41. J. Virol. 82 (2008) 10032-10041
    • (2008) J. Virol. , vol.82 , pp. 10032-10041
    • Gustchina, E.1    Bewley, C.A.2    Clore, G.M.3
  • 22
    • 14844321929 scopus 로고    scopus 로고
    • Characterization of high-affinity antibodies by electrochemiluminescence-based equilibrium titration
    • Haenel C., Satzger M., Ducata D.D., Ostendorp R., and Brocks B. Characterization of high-affinity antibodies by electrochemiluminescence-based equilibrium titration. Anal. Biochem. 339 (2005) 182-184
    • (2005) Anal. Biochem. , vol.339 , pp. 182-184
    • Haenel, C.1    Satzger, M.2    Ducata, D.D.3    Ostendorp, R.4    Brocks, B.5
  • 23
    • 16844379486 scopus 로고    scopus 로고
    • Steric accessibility of the HIV-1 gp41 N-trimer region
    • Hamburger A.E., Kim S., Welch B.D., and Kay M.S. Steric accessibility of the HIV-1 gp41 N-trimer region. J. Biol. Chem. 280 (2005) 12567-12572
    • (2005) J. Biol. Chem. , vol.280 , pp. 12567-12572
    • Hamburger, A.E.1    Kim, S.2    Welch, B.D.3    Kay, M.S.4
  • 24
    • 33746191445 scopus 로고    scopus 로고
    • Isolation and comparative characterization of Ki-67 equivalent antibodies from the HuCAL phage display library
    • Jarutat T., Frisch C., Nickels C., Merz H., and Knappik A. Isolation and comparative characterization of Ki-67 equivalent antibodies from the HuCAL phage display library. Biol. Chem. 387 (2006) 995-1003
    • (2006) Biol. Chem. , vol.387 , pp. 995-1003
    • Jarutat, T.1    Frisch, C.2    Nickels, C.3    Merz, H.4    Knappik, A.5
  • 26
    • 0031743949 scopus 로고    scopus 로고
    • A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein
    • Jiang S., Lin K., and Lu M. A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol. 72 (1998) 10213-10217
    • (1998) J. Virol. , vol.72 , pp. 10213-10217
    • Jiang, S.1    Lin, K.2    Lu, M.3
  • 27
    • 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
  • 28
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides
    • Knappik A., Ge L., Honegger A., Pack P., Fischer M., Wellnhofer G., Hoess A., Wolle J., Pluckthun A., and Virnekas B. Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J. Mol. Biol. 296 (2000) 57-86
    • (2000) J. Mol. Biol. , vol.296 , pp. 57-86
    • Knappik, A.1    Ge, L.2    Honegger, A.3    Pack, P.4    Fischer, M.5    Wellnhofer, G.6    Hoess, A.7    Wolle, J.8    Pluckthun, A.9    Virnekas, B.10
  • 31
    • 31144451337 scopus 로고    scopus 로고
    • Characterization of antibody responses elicited by human immunodeficiency virus type 1 primary isolate trimeric and monomeric envelope glycoproteins in selected adjuvants
    • Li Y., Svehla K., Mathy N.L., Voss G., Mascola J.R., and Wyatt R. Characterization of antibody responses elicited by human immunodeficiency virus type 1 primary isolate trimeric and monomeric envelope glycoproteins in selected adjuvants. J. Virol. 80 (2006) 1414-1426
    • (2006) J. Virol. , vol.80 , pp. 1414-1426
    • Li, Y.1    Svehla, K.2    Mathy, N.L.3    Voss, G.4    Mascola, J.R.5    Wyatt, R.6
  • 32
    • 0035800816 scopus 로고    scopus 로고
    • CCG-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity
    • CCG-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity. J. Biol. Chem. 276 (2001) 29485-29489
    • (2001) J. Biol. Chem. , vol.276 , pp. 29485-29489
    • Louis, J.M.1    Bewley, C.A.2    Clore, G.M.3
  • 33
    • 0037490139 scopus 로고    scopus 로고
    • Covalent trimers of the internal N-terminal trimeric coiled-coil of gp41 and antibodies directed against them are potent inhibitors of HIV envelope-mediated cell fusion
    • Louis J.M., Nesheiwat I., Chang L., Clore G.M., and Bewley C.A. Covalent trimers of the internal N-terminal trimeric coiled-coil of gp41 and antibodies directed against them are potent inhibitors of HIV envelope-mediated cell fusion. J. Biol. Chem. 278 (2003) 20278-20285
    • (2003) J. Biol. Chem. , vol.278 , pp. 20278-20285
    • Louis, J.M.1    Nesheiwat, I.2    Chang, L.3    Clore, G.M.4    Bewley, C.A.5
  • 34
    • 27144451245 scopus 로고    scopus 로고
    • Characterization and HIV-1 fusion inhibitory properties of monoclonal Fabs obtained from a human non-immune phage library selected against diverse epitopes of the ectodomain of HIV-1 gp41
    • Louis J.M., Bewley C.A., Gustchina E., Aniana A., and Clore G.M. Characterization and HIV-1 fusion inhibitory properties of monoclonal Fabs obtained from a human non-immune phage library selected against diverse epitopes of the ectodomain of HIV-1 gp41. J. Mol. Biol. 353 (2005) 945-951
    • (2005) J. Mol. Biol. , vol.353 , pp. 945-951
    • Louis, J.M.1    Bewley, C.A.2    Gustchina, E.3    Aniana, A.4    Clore, G.M.5
  • 36
    • 23244467373 scopus 로고    scopus 로고
    • Recommendations for the design and use of standard virus panels to assess neutralizing antibody responses elicited by candidate human immunodeficiency virus type 1 vaccines
    • Mascola J.R., D'Souza P., Gilbert P., Hahn B.H., Haigwood N.L., Morris L., Petropoulos C.J., Polonis V.R., Sarzotti M., and Montefiori D.C. Recommendations for the design and use of standard virus panels to assess neutralizing antibody responses elicited by candidate human immunodeficiency virus type 1 vaccines. J. Virol. 79 (2005) 10103-10107
    • (2005) J. Virol. , vol.79 , pp. 10103-10107
    • Mascola, J.R.1    D'Souza, P.2    Gilbert, P.3    Hahn, B.H.4    Haigwood, N.L.5    Morris, L.6    Petropoulos, C.J.7    Polonis, V.R.8    Sarzotti, M.9    Montefiori, D.C.10
  • 38
    • 33645230933 scopus 로고    scopus 로고
    • Membrane-anchored inhibitory peptides capture human immunodeficiency virus type 1 gp41 conformations that engage the target membrane prior to fusion
    • Melikyan G.B., Egelhofer M., and von Laer D. Membrane-anchored inhibitory peptides capture human immunodeficiency virus type 1 gp41 conformations that engage the target membrane prior to fusion. J. Virol. 80 (2006) 3249-3258
    • (2006) J. Virol. , vol.80 , pp. 3249-3258
    • Melikyan, G.B.1    Egelhofer, M.2    von Laer, D.3
  • 41
    • 0033780046 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 spinoculation enhances infection through virus binding
    • O'Doherty U., Swiggard W.J., and Malim M.H. Human immunodeficiency virus type 1 spinoculation enhances infection through virus binding. J. Virol. 74 (2000) 10074-10080
    • (2000) J. Virol. , vol.74 , pp. 10074-10080
    • O'Doherty, U.1    Swiggard, W.J.2    Malim, M.H.3
  • 42
    • 0027008593 scopus 로고
    • Mono- and bivalent antibody fragments produced in Escherichia coli: engineering, folding and antigen binding
    • Pluckthun A. Mono- and bivalent antibody fragments produced in Escherichia coli: engineering, folding and antigen binding. Immunol. Rev. 130 (1992) 151-188
    • (1992) Immunol. Rev. , vol.130 , pp. 151-188
    • Pluckthun, A.1
  • 45
    • 2442625211 scopus 로고    scopus 로고
    • HIV-1 gp41 as a target for viral entry inhibition
    • Root M.J., and Steger H.K. HIV-1 gp41 as a target for viral entry inhibition. Curr. Pharm. Des. 10 (2004) 1805-1825
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 1805-1825
    • Root, M.J.1    Steger, H.K.2
  • 46
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root M.J., Kay M.S., and Kim P.S. Protein design of an HIV-1 entry inhibitor. Science 291 (2001) 884-888
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 48
    • 33748741296 scopus 로고    scopus 로고
    • Kinetic dependence to HIV-1 entry inhibition
    • Steger H.K., and Root M.J. Kinetic dependence to HIV-1 entry inhibition. J. Biol. Chem. 281 (2006) 25813-25821
    • (2006) J. Biol. Chem. , vol.281 , pp. 25813-25821
    • Steger, H.K.1    Root, M.J.2
  • 49
    • 52949093147 scopus 로고    scopus 로고
    • In vitro affinity maturation of human GM-CSF antibodies by targeted CDR-diversification
    • Steidl S., Ratsch O., Brocks B., Durr M., and Thomassen-Wolf E. In vitro affinity maturation of human GM-CSF antibodies by targeted CDR-diversification. Mol. Immunol. 46 (2008) 135-144
    • (2008) Mol. Immunol. , vol.46 , pp. 135-144
    • Steidl, S.1    Ratsch, O.2    Brocks, B.3    Durr, M.4    Thomassen-Wolf, E.5
  • 50
    • 0029020970 scopus 로고
    • Replicative function and neutralization sensitivity of envelope glycoproteins from primary and T-cell line-passaged human immunodeficiency virus type 1 isolates
    • Sullivan N., Sun Y., Li J., Hofmann W., and Sodroski J. Replicative function and neutralization sensitivity of envelope glycoproteins from primary and T-cell line-passaged human immunodeficiency virus type 1 isolates. J. Virol. 69 (1995) 4413-4422
    • (1995) J. Virol. , vol.69 , pp. 4413-4422
    • Sullivan, N.1    Sun, Y.2    Li, J.3    Hofmann, W.4    Sodroski, J.5
  • 51
  • 52
    • 0028559783 scopus 로고
    • Trinucleotide phosphoramidites: ideal reagents for the synthesis of mixed oligonucleotides for random mutagenesis
    • Virnekas B., Ge L., Pluckthun A., Schneider K.C., Wellnhofer G., and Moroney S.E. Trinucleotide phosphoramidites: ideal reagents for the synthesis of mixed oligonucleotides for random mutagenesis. Nucleic Acids Res. 22 (1994) 5600-5607
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5600-5607
    • Virnekas, B.1    Ge, L.2    Pluckthun, A.3    Schneider, K.C.4    Wellnhofer, G.5    Moroney, S.E.6
  • 54
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition
    • Wild C., Oas T., McDanal C., Bolognesi D., and Matthews T. A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 10537-10541
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 55
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild C.T., Shugars D.C., Greenwell T.K., McDanal C.B., and Matthews T.J. Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 9770-9774
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.