메뉴 건너뛰기




Volumn 47, Issue 9, 2010, Pages 1747-1756

Molecular analysis of multicatalytic monoclonal antibodies

Author keywords

Affinity; Catalytic antibody genes; Coat protein; Cucumber mosaic virus; DNase; ELISA; Monoclonal antibodies; Protease; RNase

Indexed keywords

AUTOANTIBODY; DNA ANTIBODY; DOUBLE STRANDED DNA; EPITOPE; MONOCLONAL ANTIBODY; PROTEINASE; RIBONUCLEASE; SINGLE STRANDED DNA;

EID: 77952321581     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2010.02.024     Document Type: Article
Times cited : (5)

References (57)
  • 2
    • 0034129428 scopus 로고    scopus 로고
    • Catalytic mechanism of an abzyme displaying a β-lactamase-like activity
    • Avalle B., Debat H., Friboulet A., Thomas D. Catalytic mechanism of an abzyme displaying a β-lactamase-like activity. Appl. Biochem. Biotechnol. 2000, 83:163-169.
    • (2000) Appl. Biochem. Biotechnol. , vol.83 , pp. 163-169
    • Avalle, B.1    Debat, H.2    Friboulet, A.3    Thomas, D.4
  • 5
    • 0016311758 scopus 로고
    • Do immunoglobulins have proteolytic activity?
    • Erhan S., Greller L.D. Do immunoglobulins have proteolytic activity?. Nature 1974, 251:353-355.
    • (1974) Nature , vol.251 , pp. 353-355
    • Erhan, S.1    Greller, L.D.2
  • 6
    • 0031945007 scopus 로고    scopus 로고
    • Evolving catalytic antibodies in a phage-displayed combinatorial library
    • Fujii I., Fukuyama S., Iwabuchi Y., Tanimura R. Evolving catalytic antibodies in a phage-displayed combinatorial library. Nat. Biotechnol. 1998, 16:463-467.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 463-467
    • Fujii, I.1    Fukuyama, S.2    Iwabuchi, Y.3    Tanimura, R.4
  • 7
    • 0028794728 scopus 로고
    • Correlation between antigen-combining-site structures and functions within a panel of catalytic antibodies generated against a single transition state analog
    • Fujii I., Tanaka F., Miyashita H., Tanimura R., Kinoshita K. Correlation between antigen-combining-site structures and functions within a panel of catalytic antibodies generated against a single transition state analog. J. Am. Chem. Soc. 1995, 117:6199-6209.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6199-6209
    • Fujii, I.1    Tanaka, F.2    Miyashita, H.3    Tanimura, R.4    Kinoshita, K.5
  • 10
    • 0003448569 scopus 로고
    • Antibodies
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow E., Lane D. Antibodies. A Laboratory Manual 1988, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 11
    • 0036837369 scopus 로고    scopus 로고
    • Targeted destruction of the HIV-1 coat protein gp41 by a catalytic antibody light chain
    • Hifumi E., Mitsuda Y., Ohara K., Uda T. Targeted destruction of the HIV-1 coat protein gp41 by a catalytic antibody light chain. J. Immunol. Methods 2002, 269:283-298.
    • (2002) J. Immunol. Methods , vol.269 , pp. 283-298
    • Hifumi, E.1    Mitsuda, Y.2    Ohara, K.3    Uda, T.4
  • 13
    • 0024584482 scopus 로고
    • Sequence-specific peptide cleavage catalyzed by an antibody
    • Iverson B.L., Lerner R.A. Sequence-specific peptide cleavage catalyzed by an antibody. Science 1989, 243:1184-1188.
    • (1989) Science , vol.243 , pp. 1184-1188
    • Iverson, B.L.1    Lerner, R.A.2
  • 14
    • 0027489204 scopus 로고
    • Monoclonal anti-idiotypic antibodies as functional internal images of enzyme active sites. Production of a catalytic antibody with a cholinesterase activity
    • Izadyar L., Friboulet A., Remy M.H., Roseto A., Thomas D. Monoclonal anti-idiotypic antibodies as functional internal images of enzyme active sites. Production of a catalytic antibody with a cholinesterase activity. Proc. Natl. Acad. Sci. U.S.A. 1993, 90:8876-8880.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 8876-8880
    • Izadyar, L.1    Friboulet, A.2    Remy, M.H.3    Roseto, A.4    Thomas, D.5
  • 15
    • 0037298948 scopus 로고    scopus 로고
    • Anti-DNA antibodies: aspects of structure and pathogenicity
    • Jang Y.J., Stollar B.D. Anti-DNA antibodies: aspects of structure and pathogenicity. Cell. Mol. Life Sci. 2003, 60:309-320.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 309-320
    • Jang, Y.J.1    Stollar, B.D.2
  • 17
    • 58149496086 scopus 로고    scopus 로고
    • Generation of humanized anti-DNA hydrolyzing catalytic antibodies by complementarity determining region grafting Biochem
    • Kim D.S., Lee S.H., Kim J.S., Lee S.C., Kwon M.H., Kim Y.S. Generation of humanized anti-DNA hydrolyzing catalytic antibodies by complementarity determining region grafting Biochem. Biophys. Res. Commun. 2009, 379(2):314-318.
    • (2009) Biophys. Res. Commun. , vol.379 , Issue.2 , pp. 314-318
    • Kim, D.S.1    Lee, S.H.2    Kim, J.S.3    Lee, S.C.4    Kwon, M.H.5    Kim, Y.S.6
  • 18
    • 33744962513 scopus 로고    scopus 로고
    • Heavy and light chain variable single domains of an anti-DNA binding antibody hydrolyze both double- and single-stranded DNAs without sequence specificity
    • Kim Y.R., Kim J.S., Lee S.H., Lee W.R., Sohn J.N., Chung Y.C., Shim H.K., Lee S.C., Kwon M.H., Kim Y.S. Heavy and light chain variable single domains of an anti-DNA binding antibody hydrolyze both double- and single-stranded DNAs without sequence specificity. J. Biol. Chem. 2006, 281:15287-15295.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15287-15295
    • Kim, Y.R.1    Kim, J.S.2    Lee, S.H.3    Lee, W.R.4    Sohn, J.N.5    Chung, Y.C.6    Shim, H.K.7    Lee, S.C.8    Kwon, M.H.9    Kim, Y.S.10
  • 24
    • 0032425580 scopus 로고    scopus 로고
    • Conversion of an antibody into an enzyme which cleaves the protein HPr
    • Liu E., Prasad L., Delbaere L.T., Waygood E.B., Lee J.S. Conversion of an antibody into an enzyme which cleaves the protein HPr. Mol. Immunol. 1998, 35(16):1069-1077.
    • (1998) Mol. Immunol. , vol.35 , Issue.16 , pp. 1069-1077
    • Liu, E.1    Prasad, L.2    Delbaere, L.T.3    Waygood, E.B.4    Lee, J.S.5
  • 25
    • 0036776323 scopus 로고    scopus 로고
    • A Conserved capsid protein surface domain of Cucumber mosaic virus is essential for efficient aphid vector transmission
    • Liu S., He X., Park G., Josefsson C., Perry K.L. A Conserved capsid protein surface domain of Cucumber mosaic virus is essential for efficient aphid vector transmission. J. Virol. 2002, 76:9756-9762.
    • (2002) J. Virol. , vol.76 , pp. 9756-9762
    • Liu, S.1    He, X.2    Park, G.3    Josefsson, C.4    Perry, K.L.5
  • 26
    • 0032560498 scopus 로고    scopus 로고
    • Antibody catalysis of peptidyl-prolyl cis-trans isomerization in the folding of RNase T1
    • Ma L., Hsieh-Wilson L.C., Schultz P.G. Antibody catalysis of peptidyl-prolyl cis-trans isomerization in the folding of RNase T1. Proc. Natl. Acad. Sci. U.S.A. 1998, 95(13):7251-7256.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , Issue.13 , pp. 7251-7256
    • Ma, L.1    Hsieh-Wilson, L.C.2    Schultz, P.G.3
  • 27
    • 0030916550 scopus 로고    scopus 로고
    • Monoclonal Anti-DNA Antibodies: structure, specificity, and biology
    • Marion T.N., Krishnan M.R., Desai D.D., Jou N.T., Tillman D.M. Monoclonal Anti-DNA Antibodies: structure, specificity, and biology. Methods 1997, 11:3-11.
    • (1997) Methods , vol.11 , pp. 3-11
    • Marion, T.N.1    Krishnan, M.R.2    Desai, D.D.3    Jou, N.T.4    Tillman, D.M.5
  • 30
    • 1842578276 scopus 로고    scopus 로고
    • Catalytic antibody light chain capable of cleaving a chemokine receptor CCR-5 peptide with a high reaction rate constant
    • Mitsuda Y., Hifumi E., Tsuruhata K., Fujinami H., Yamamoto N., Uda T. Catalytic antibody light chain capable of cleaving a chemokine receptor CCR-5 peptide with a high reaction rate constant. Biotechnol. Bioeng. 2004, 86:217-225.
    • (2004) Biotechnol. Bioeng. , vol.86 , pp. 217-225
    • Mitsuda, Y.1    Hifumi, E.2    Tsuruhata, K.3    Fujinami, H.4    Yamamoto, N.5    Uda, T.6
  • 31
    • 0031576985 scopus 로고    scopus 로고
    • Site-directed mutagenesis of active site contact residues in a hydrolytic abzyme: evidence for an essential histidine involved in transition state stabilization
    • Miyashita H., Hara T., Tanimura R., Fukuyama S., Cagnon C., Kohara A., Fujii I. Site-directed mutagenesis of active site contact residues in a hydrolytic abzyme: evidence for an essential histidine involved in transition state stabilization. J. Mol. Biol. 1997, 267:1247-1257.
    • (1997) J. Mol. Biol. , vol.267 , pp. 1247-1257
    • Miyashita, H.1    Hara, T.2    Tanimura, R.3    Fukuyama, S.4    Cagnon, C.5    Kohara, A.6    Fujii, I.7
  • 32
    • 0028292036 scopus 로고
    • A common ancestry for multiple catalytic antibodies generated against a single transition-state analog
    • Miyashita H., Hara T., Tanimura R., Tanaka F., Kikuchi M., Fujii I. A common ancestry for multiple catalytic antibodies generated against a single transition-state analog. Proc. Natl. Acad. Sci. U.S.A. 1994, 91:6045-6049.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 6045-6049
    • Miyashita, H.1    Hara, T.2    Tanimura, R.3    Tanaka, F.4    Kikuchi, M.5    Fujii, I.6
  • 33
    • 0021915799 scopus 로고
    • Nucleic acid structure and expression of the human AIDS/lymphadenopathy retrovirus
    • Muesing M.A., Smith D.H., Cabradilla C.D., Benton C.V., Lasky L.A., Capon D.J. Nucleic acid structure and expression of the human AIDS/lymphadenopathy retrovirus. Nature 1985, 313(6002):450-458.
    • (1985) Nature , vol.313 , Issue.6002 , pp. 450-458
    • Muesing, M.A.1    Smith, D.H.2    Cabradilla, C.D.3    Benton, C.V.4    Lasky, L.A.5    Capon, D.J.6
  • 34
    • 0035823022 scopus 로고    scopus 로고
    • Complement-independent, peroxide-induced antibody lysis of platelets in HIV-1-related immune thrombocytopenia
    • Nardi M., Tomlinson S., Greco M.A., Karpatkin S. Complement-independent, peroxide-induced antibody lysis of platelets in HIV-1-related immune thrombocytopenia. Cell 2001, 106:551.
    • (2001) Cell , vol.106 , pp. 551
    • Nardi, M.1    Tomlinson, S.2    Greco, M.A.3    Karpatkin, S.4
  • 35
    • 0036837151 scopus 로고    scopus 로고
    • Human catalytic RNA- and DNA-hydrolyzing antibodies
    • Nevinsky G.A., Buneva V.N. Human catalytic RNA- and DNA-hydrolyzing antibodies. J. Immunol. Methods 2002, 269:235-249.
    • (2002) J. Immunol. Methods , vol.269 , pp. 235-249
    • Nevinsky, G.A.1    Buneva, V.N.2
  • 37
    • 0242661543 scopus 로고    scopus 로고
    • DNA-specific autoantibody cleaves DNA by hydrolysis of phosphodiester and glycosidic bond
    • Nguyen H.T.T., Jang Y.J., Jeong S., Yu J. DNA-specific autoantibody cleaves DNA by hydrolysis of phosphodiester and glycosidic bond. Biochem. Biophys. Res. Commun. 2003, 311:767-773.
    • (2003) Biochem. Biophys. Res. Commun. , vol.311 , pp. 767-773
    • Nguyen, H.T.T.1    Jang, Y.J.2    Jeong, S.3    Yu, J.4
  • 41
    • 0024382917 scopus 로고
    • Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody
    • Paul S., Volle D.J., Beach C.M., Johnson D.R., Powell M.J., Massey R.J. Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody. Science 1989, 244:1158-1162.
    • (1989) Science , vol.244 , pp. 1158-1162
    • Paul, S.1    Volle, D.J.2    Beach, C.M.3    Johnson, D.R.4    Powell, M.J.5    Massey, R.J.6
  • 46
    • 0025669926 scopus 로고
    • Purification and characterisation of an extracellular serine proteinase from Aspergillus fumigatus and its detection in tissue
    • Reichard U., Buttner S., Eiffert H., Staib F., Ruchel R. Purification and characterisation of an extracellular serine proteinase from Aspergillus fumigatus and its detection in tissue. J. Med. Microbiol. 1990, 33:243-251.
    • (1990) J. Med. Microbiol. , vol.33 , pp. 243-251
    • Reichard, U.1    Buttner, S.2    Eiffert, H.3    Staib, F.4    Ruchel, R.5
  • 47
    • 0032549776 scopus 로고    scopus 로고
    • Immunological origins of binding and catalysis in a Diels-Alderase antibody
    • Romesberg F.E., Spiller B., Schultz P.G., Stevens R.C. Immunological origins of binding and catalysis in a Diels-Alderase antibody. Science 1998, 279:1929-1933.
    • (1998) Science , vol.279 , pp. 1929-1933
    • Romesberg, F.E.1    Spiller, B.2    Schultz, P.G.3    Stevens, R.C.4
  • 50
    • 0035011047 scopus 로고    scopus 로고
    • In vitro abzyme evolution to optimize antibody recognition for catalysis
    • Takahashi N., Kakinuma H., Liu L., Nishi Y., Fujii I. In vitro abzyme evolution to optimize antibody recognition for catalysis. Nat. Biotechnol. 2001, 19(6):563-567.
    • (2001) Nat. Biotechnol. , vol.19 , Issue.6 , pp. 563-567
    • Takahashi, N.1    Kakinuma, H.2    Liu, L.3    Nishi, Y.4    Fujii, I.5
  • 51
    • 0028910170 scopus 로고
    • Unexpected high occurrence of catalytic antibodies in MRL/lpr and SJL mice immunized with a transition-state analog: is there a linkage to autoimmunity?
    • Tawfik D.S., Chap R., Green B.S., Sela M., Eshhar Z. Unexpected high occurrence of catalytic antibodies in MRL/lpr and SJL mice immunized with a transition-state analog: is there a linkage to autoimmunity?. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:2145-2149.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 2145-2149
    • Tawfik, D.S.1    Chap, R.2    Green, B.S.3    Sela, M.4    Eshhar, Z.5
  • 52
    • 0033821422 scopus 로고    scopus 로고
    • Prothrombin cleaving antibody light chains
    • Thiagarajan P., Paul S. Prothrombin cleaving antibody light chains. Chem. Immunol. 2000, 77:115-129.
    • (2000) Chem. Immunol. , vol.77 , pp. 115-129
    • Thiagarajan, P.1    Paul, S.2
  • 53
    • 0029030145 scopus 로고
    • An approach for an immunoaffinity AIDS sensor using the conservative region of the HIV envelope protein (gp41) and its monoclonal antibody
    • Uda T., Hifumi E., Kobayashi T., Shimizu K., Sata T., Ogino K. An approach for an immunoaffinity AIDS sensor using the conservative region of the HIV envelope protein (gp41) and its monoclonal antibody. Biosens. Bioelectron. 1995, 10(5):477-483.
    • (1995) Biosens. Bioelectron. , vol.10 , Issue.5 , pp. 477-483
    • Uda, T.1    Hifumi, E.2    Kobayashi, T.3    Shimizu, K.4    Sata, T.5    Ogino, K.6
  • 54
    • 0033811670 scopus 로고    scopus 로고
    • Catalytic activity of antibody light chain to gp41: a consideration of refolding in relation to activation mechanism
    • Uda T., Hifumi E., Ohara K., Yan Z. Catalytic activity of antibody light chain to gp41: a consideration of refolding in relation to activation mechanism. Chem. Immunol. 2000, 77:18-32.
    • (2000) Chem. Immunol. , vol.77 , pp. 18-32
    • Uda, T.1    Hifumi, E.2    Ohara, K.3    Yan, Z.4
  • 57
    • 62749193777 scopus 로고    scopus 로고
    • Monoclonal antibodies specific to Cucumber mosaic virus coat protein possess DNA-hydrolyzing activity
    • Zein H.S., Teixeira da Silva J.A., Miyatake K. Monoclonal antibodies specific to Cucumber mosaic virus coat protein possess DNA-hydrolyzing activity. Mol. Immunol. 2009, 46:1527-1533.
    • (2009) Mol. Immunol. , vol.46 , pp. 1527-1533
    • Zein, H.S.1    Teixeira da Silva, J.A.2    Miyatake, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.