메뉴 건너뛰기




Volumn 414, Issue 4, 2011, Pages 545-562

In vitro affinity maturation of an anti-PSA antibody for prostate cancer diagnostic assay

Author keywords

affinity engineering; hot spots; phage display; prostate specific antigen; scFv antibody fragment

Indexed keywords

DNA; IMMUNOGLOBULIN F(AB) FRAGMENT; PROSTATE SPECIFIC ANTIGEN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY;

EID: 82555168293     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.10.008     Document Type: Article
Times cited : (16)

References (48)
  • 1
    • 0023218055 scopus 로고
    • Molecular cloning of human prostate specific antigen cDNA
    • DOI 10.1016/0014-5793(87)80078-9
    • Lundwall A., and Lilja H. Molecular cloning of human prostate specific antigen cDNA FEBS Lett. 214 1987 317 322 (Pubitemid 17085741)
    • (1987) FEBS Letters , vol.214 , Issue.2 , pp. 317-322
    • Lundwall, A.1    Lilja, H.2
  • 2
    • 0022357088 scopus 로고
    • A kallikrein-like serine protease in prostatic fluid cleaves the predominant seminal vesicle protein
    • Lilja H. A kallikrein-like serine protease in prostatic fluid cleaves the predominant seminal vesicle protein J. Clin. Invest. 76 1985 1899 1903 (Pubitemid 16196061)
    • (1985) Journal of Clinical Investigation , vol.76 , Issue.5 , pp. 1899-1903
    • Lilja, H.1
  • 3
    • 0028865036 scopus 로고
    • Prostate-specific antigen, a serine protease, facilitates human prostate cancer cell invasion
    • Webber M.M., Waghray A., and Bello D. Prostate-specific antigen, a serine protease, facilitates human prostate cancer cell invasion Clin. Cancer Res. 1 1995 1089 1094
    • (1995) Clin. Cancer Res. , vol.1 , pp. 1089-1094
    • Webber, M.M.1    Waghray, A.2    Bello, D.3
  • 5
    • 0023233060 scopus 로고
    • Prostate-specific antigen as a serum marker for adenocarcinoma of the prostate
    • Stamey T.A., Yang N., Hay A.R., McNeal J.E., Freiha F.S., and Redwine E. Prostate-specific antigen as a serum marker for adenocarcinoma of the prostate N. Engl. J. Med. 317 1987 909 916 (Pubitemid 17147932)
    • (1987) New England Journal of Medicine , vol.317 , Issue.15 , pp. 909-916
    • Stamey, T.A.1    Yang, N.2    Hay, A.R.3
  • 6
    • 0025671852 scopus 로고
    • Enzymatic activity of prostate-specific antigen and its reactions with extracellular serine proteinase inhibitors
    • Christensson A., Laurell C.B., and Lilja H. Enzymatic activity of prostate-specific antigen and its reactions with extracellular serine proteinase inhibitors Eur. J. Biochem. 194 1990 755 763
    • (1990) Eur. J. Biochem. , vol.194 , pp. 755-763
    • Christensson, A.1    Laurell, C.B.2    Lilja, H.3
  • 8
    • 0037235237 scopus 로고    scopus 로고
    • 1-antichymotrypsin complex together with free or total PSA
    • DOI 10.1373/49.1.97
    • Zhu L., Leinonen J., Zhang W.M., Finne P., and Stenman U.H. Dual-label immunoassay for simultaneous measurement of prostate-specific antigen (PSA)-alpha1-antichymotrypsin complex together with free or total PSA Clin. Chem. 49 2003 97 103 (Pubitemid 36078558)
    • (2003) Clinical Chemistry , vol.49 , Issue.1 , pp. 97-103
    • Zhu, L.1    Leinonen, J.2    Zhang, W.-M.3    Finne, P.4    Stenman, U.-H.5
  • 9
    • 1642533463 scopus 로고    scopus 로고
    • Immunopeptidometric Assay for Enzymatically Active Prostate-Specific Antigen
    • DOI 10.1373/clinchem.2003.026146
    • Wu P., Zhu L., Stenman U.H., and Leinonen J. Immunopeptidometric assay for enzymatically active prostate-specific antigen Clin. Chem. 50 2004 125 129 (Pubitemid 38125708)
    • (2004) Clinical Chemistry , vol.50 , Issue.1 , pp. 125-129
    • Wu, P.1    Zhu, L.2    Stenman, U.-H.3    Leinonen, J.4
  • 10
    • 0028828899 scopus 로고
    • Measurement of the proportion of free to total prostate-specific antigen improves diagnostic performance of prostate-specific antigen in the diagnostic gray zone of total prostate-specific antigen
    • Luderer A.A., Chen Y.T., Soriano T.F., Kramp W.J., Carlson G., and Cuny C. Measurement of the proportion of free to total prostate-specific antigen improves diagnostic performance of prostate-specific antigen in the diagnostic gray zone of total prostate-specific antigen Urology 46 1995 187 194
    • (1995) Urology , vol.46 , pp. 187-194
    • Luderer, A.A.1    Chen, Y.T.2    Soriano, T.F.3    Kramp, W.J.4    Carlson, G.5    Cuny, C.6
  • 14
    • 0037235949 scopus 로고    scopus 로고
    • Engineered antibodies
    • DOI 10.1038/nm0103-129
    • Hudson P.J., and Souriau C. Engineered antibodies Nat. Med. 9 2003 129 134 (Pubitemid 36098274)
    • (2003) Nature Medicine , vol.9 , Issue.1 , pp. 129-134
    • Hudson, P.J.1    Souriau, C.2
  • 15
    • 33646146483 scopus 로고    scopus 로고
    • Affinity enhancement of an in vivo matured therapeutic antibody using structure-based computational design
    • Clark L.A., Boriack-Sjodin P.A., Eldredge J., Fitch C., Friedman B., and Hanf K.J. Affinity enhancement of an in vivo matured therapeutic antibody using structure-based computational design Protein Sci. 15 2006 949 960
    • (2006) Protein Sci. , vol.15 , pp. 949-960
    • Clark, L.A.1    Boriack-Sjodin, P.A.2    Eldredge, J.3    Fitch, C.4    Friedman, B.5    Hanf, K.J.6
  • 16
    • 0027184954 scopus 로고
    • Phage display and selection of a site-directed randomized single-chain antibody Fv fragment for its affinity improvement
    • Riechmann L., and Weill M. Phage display and selection of a site-directed randomized single-chain antibody Fv fragment for its affinity improvement Biochemistry 32 1993 8848 8855 (Pubitemid 23268808)
    • (1993) Biochemistry , vol.32 , Issue.34 , pp. 8848-8855
    • Riechmann, L.1    Weill, M.2
  • 18
    • 0033056238 scopus 로고    scopus 로고
    • Improving antibody affinity by mimicking somatic hypermutation in vitro
    • DOI 10.1038/9872
    • Chowdhury P.S., and Pastan I. Improving antibody affinity by mimicking somatic hypermutation in vitro Nat. Biotechnol. 17 1999 568 572 (Pubitemid 29262920)
    • (1999) Nature Biotechnology , vol.17 , Issue.6 , pp. 568-572
    • Chowdhury, P.S.1    Pastan, I.2
  • 20
    • 0033927216 scopus 로고    scopus 로고
    • Immunotoxins with increased activity against epidermal growth factor receptor vIII-expressing cells produced by antibody phage display
    • Beers R., Chowdhury P., Bigner D., and Pastan I. Immunotoxins with increased activity against epidermal growth factor receptor vIII-expressing cells produced by antibody phage display Clin. Cancer Res. 6 2000 2835 2843 (Pubitemid 30482125)
    • (2000) Clinical Cancer Research , vol.6 , Issue.7 , pp. 2835-2843
    • Beers, R.1    Chowdhury, P.2    Bigner, D.3    Pastan, I.4
  • 21
    • 0036554968 scopus 로고    scopus 로고
    • Improved cytotoxic activity toward cell lines and fresh leukemia cells of a mutant anti-CD22 immunotoxin obtained by antibody phage display
    • Salvatore G., Beers R., Margulies I., Kreitman R.J., and Pastan I. Improved cytotoxic activity toward cell lines and fresh leukemia cells of a mutant anti-CD22 immunotoxin obtained by antibody phage display Clin. Cancer Res. 8 2002 995 1002 (Pubitemid 35177347)
    • (2002) Clinical Cancer Research , vol.8 , Issue.4 , pp. 995-1002
    • Salvatore, G.1    Beers, R.2    Margulies, I.3    Kreitman, R.J.4    Pastan, I.5
  • 22
    • 12844267487 scopus 로고    scopus 로고
    • In vitro antibody evolution targeting germline hot spots to increase activity of an anti-CD22 immunotoxin
    • DOI 10.1074/jbc.M409783200
    • Ho M., Kreitman R.J., Onda M., and Pastan I. In vitro antibody evolution targeting germline hot spots to increase activity of an anti-CD22 immunotoxin J. Biol. Chem. 280 2005 607 617 (Pubitemid 40165027)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.1 , pp. 607-617
    • Ho, M.1    Kreitman, R.J.2    Onda, M.3    Pastan, I.4
  • 25
    • 0042346235 scopus 로고    scopus 로고
    • Antibody repertoire and gene expression profile: Implications for different developmental and functional traits of splenic and peritoneal B-1 lymphocytes
    • Kretschmer K., Jungebloud A., Stopkowicz J., Stoermann B., Hoffmann R., and Weiss S. Antibody repertoire and gene expression profile: implications for different developmental and functional traits of splenic and peritoneal B-1 lymphocytes J. Immunol. 171 2003 1192 1201 (Pubitemid 36900047)
    • (2003) Journal of Immunology , vol.171 , Issue.3 , pp. 1192-1201
    • Kretschmer, K.1    Jungebloud, A.2    Stopkowicz, J.3    Stoermann, B.4    Hoffmann, R.5    Weiss, S.6
  • 28
    • 0034718592 scopus 로고    scopus 로고
    • Breaking the affinity ceiling for antibodies and T cell receptors
    • Foote J., and Eisen H.N. Breaking the affinity ceiling for antibodies and T cell receptors Proc. Natl Acad. Sci. USA 97 2000 10679 10681
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10679-10681
    • Foote, J.1    Eisen, H.N.2
  • 29
    • 0036686414 scopus 로고    scopus 로고
    • 315 transgenic mice
    • DOI 10.1002/1521-4141(200208)32:8<2317::AID-IMMU2317>3.0.CO;2-0
    • Kretschmer K., Engel H., and Weiss S. Strong antigenic selection shaping the immunoglobulin heavy chain repertoire of B-1a lymphocytes in lambda 2(315) transgenic mice Eur. J. Immunol. 32 2002 2317 2327 (Pubitemid 34965895)
    • (2002) European Journal of Immunology , vol.32 , Issue.8 , pp. 2317-2327
    • Kretschmer, K.1    Engel, H.2    Weiss, S.3
  • 30
    • 0036238393 scopus 로고    scopus 로고
    • Specificity mapping of human anti-T cell receptor monoclonal natural antibodies: Defining the properties of epitope recognition promiscuity
    • DOI 10.1096/fj.01-0884com
    • Robey I.F., Edmundson A.B., Schluter S.F., Yocum D.E., and Marchalonis J.J. Specificity mapping of human anti-T cell receptor monoclonal natural antibodies: defining the properties of epitope recognition promiscuity FASEB J. 16 2002 642 652 (Pubitemid 34465428)
    • (2002) FASEB Journal , vol.16 , Issue.7 , pp. 642-652
    • Robey, I.F.1    Edmundson, A.B.2    Schluter, S.F.3    Yocum, D.E.4    Marchalonis, J.J.5
  • 31
    • 0030580057 scopus 로고    scopus 로고
    • Antibody-antigen interactions: Contact analysis and binding site topography
    • DOI 10.1006/jmbi.1996.0548
    • MacCallum R.M., Martin A.C., and Thornton J.M. Antibody-antigen interactions: contact analysis and binding site topography J. Mol. Biol. 262 1996 732 745 (Pubitemid 26343518)
    • (1996) Journal of Molecular Biology , vol.262 , Issue.5 , pp. 732-745
    • MacCallum, R.M.1    Martin, A.C.R.2    Thornton, J.M.3
  • 33
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • DOI 10.1038/370389a0
    • Stemmer W.P. Rapid evolution of a protein in vitro by DNA shuffling Nature 370 1994 389 391 (Pubitemid 24259765)
    • (1994) Nature , vol.370 , Issue.6488 , pp. 389-391
    • Stemmer, W.P.C.1
  • 34
    • 0029564921 scopus 로고
    • CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range
    • DOI 10.1006/jmbi.1995.0626
    • Yang W.P., Green K., Pinz-Sweeney S., Briones A.T., Burton D.R., and Barbas C.F. CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range J. Mol. Biol. 254 1995 392 403 (Pubitemid 26001779)
    • (1995) Journal of Molecular Biology , vol.254 , Issue.3 , pp. 392-403
    • Yang, W.-P.1    Green, K.2    Pinz-Sweeney, S.3    Briones, A.T.4    Burton, D.R.5    Barbas III, C.F.6
  • 35
    • 0028348564 scopus 로고
    • In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity
    • Barbas C.F. 3rd, Hu D., Dunlop N., Sawyer L., Cababa D., and Hendry R.M. In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity Proc. Natl Acad. Sci. USA 91 1994 3809 3813
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3809-3813
    • Barbas III, C.F.1    Hu, D.2    Dunlop, N.3    Sawyer, L.4    Cababa, D.5    Hendry, R.M.6
  • 36
    • 0030200088 scopus 로고    scopus 로고
    • Selection and evolution of high-affinity human anti-viral antibodies
    • DOI 10.1016/0167-7799(96)10029-9
    • Barbas C.F. 3rd, and Burton D.R. Selection and evolution of high-affinity human anti-viral antibodies Trends Biotechnol. 14 1996 230 234 (Pubitemid 26251772)
    • (1996) Trends in Biotechnology , vol.14 , Issue.7 , pp. 230-234
    • Barbas III, C.F.1    Burton, D.R.2
  • 37
    • 44849121670 scopus 로고    scopus 로고
    • Affinity maturation of tacrolimus antibody for improved immunoassay performance
    • DOI 10.1373/clinchem.2007.097352
    • Siegel R.W., Baugher W., Rahn T., Drengler S., and Tyner J. Affinity maturation of tacrolimus antibody for improved immunoassay performance Clin. Chem. 54 2008 1008 1017 (Pubitemid 351793407)
    • (2008) Clinical Chemistry , vol.54 , Issue.6 , pp. 1008-1017
    • Siegel, R.W.1    Baugher, W.2    Rahn, T.3    Drengler, S.4    Tyner, J.5
  • 38
    • 17044431976 scopus 로고    scopus 로고
    • Use of an in vivo biotinylated single-chain antibody as capture reagent in an immunometric assay to decrease the incidence of interference from heterophilic antibodies
    • DOI 10.1373/clinchem.2004.046979
    • Warren D.J., Bjerner J., Paus E., Bormer O.P., and Nustad K. Use of an in vivo biotinylated single-chain antibody as capture reagent in an immunometric assay to decrease the incidence of interference from heterophilic antibodies Clin. Chem. 51 2005 830 838 (Pubitemid 40577919)
    • (2005) Clinical Chemistry , vol.51 , Issue.5 , pp. 830-838
    • Warren, D.J.1    Bjerner, J.2    Paus, E.3    Bormer, O.P.4    Nustad, K.5
  • 39
    • 17744391988 scopus 로고    scopus 로고
    • Improving immunoassay performance by antibody engineering
    • Stenman U.H. Improving immunoassay performance by antibody engineering Clin. Chem. 51 2005 801 802
    • (2005) Clin. Chem. , vol.51 , pp. 801-802
    • Stenman, U.H.1
  • 40
    • 77956923750 scopus 로고    scopus 로고
    • Coevolution of antibody stability and Vkappa CDR-L3 canonical structure
    • Luo J., Obmolova G., Huang A., Strake B., Teplyakov A., and Malia T. Coevolution of antibody stability and Vkappa CDR-L3 canonical structure J. Mol. Biol. 402 2010 708 719
    • (2010) J. Mol. Biol. , vol.402 , pp. 708-719
    • Luo, J.1    Obmolova, G.2    Huang, A.3    Strake, B.4    Teplyakov, A.5    Malia, T.6
  • 41
    • 48449094247 scopus 로고    scopus 로고
    • IMGT/V-QUEST: The highly customized and integrated system for IG and TR standardized V-J and V-D-J sequence analysis
    • Brochet X., Lefranc M.P., and Giudicelli V. IMGT/V-QUEST: the highly customized and integrated system for IG and TR standardized V-J and V-D-J sequence analysis Nucleic Acids Res. 36 2008 W503 W508
    • (2008) Nucleic Acids Res. , vol.36
    • Brochet, X.1    Lefranc, M.P.2    Giudicelli, V.3
  • 42
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • DOI 10.1016/0378-1119(89)90359-4
    • Horton R.M., Hunt H.D., Ho S.N., Pullen J.K., and Pease L.R. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension Gene 77 1989 61 68 (Pubitemid 19125654)
    • (1989) Gene , vol.77 , Issue.1 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 44
    • 0031032155 scopus 로고    scopus 로고
    • Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system
    • DOI 10.1016/S0022-1759(96)00208-6, PII S0022175996002086
    • Krebber A., Bornhauser S., Burmester J., Honegger A., Willuda J., Bosshard H.R., and Pluckthun A. Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system J. Immunol. Methods 201 1997 35 55 (Pubitemid 27072663)
    • (1997) Journal of Immunological Methods , vol.201 , Issue.1 , pp. 35-55
    • Krebber, A.1    Bornhauser, S.2    Burmester, J.3    Honegger, A.4    Willuda, J.5    Bosshard, H.R.6    Pluckthun, A.7
  • 45
    • 33646918138 scopus 로고    scopus 로고
    • Affinity maturation of phage antibodies
    • T. Clackson, H.B. Lowman, Oxford University Press Oxford, UK
    • Nielsen U.B., and Marks J.D. Affinity maturation of phage antibodies T. Clackson, H.B. Lowman, Phage Display: A Practical Approach 2004 Oxford University Press Oxford, UK
    • (2004) Phage Display: A Practical Approach
    • Nielsen, U.B.1    Marks, J.D.2
  • 46
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
    • Karlsson R., Michaelsson A., and Mattsson L. Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system J. Immunol. Methods 145 1991 229 240
    • (1991) J. Immunol. Methods , vol.145 , pp. 229-240
    • Karlsson, R.1    Michaelsson, A.2    Mattsson, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.