메뉴 건너뛰기




Volumn 21, Issue 6, 1998, Pages 399-408

Peptide vaccination with an anchor-replaced CTL epitope protects against human papillomavirus type 16-induced tumors expressing the wild-type epitope

Author keywords

Anchor replacement; Cytotoxic T lymphocytes; Human papillomavirus type 16; Peptide; Vaccine

Indexed keywords

CARRIER PROTEIN; EPITOPE; EUROPIUM; FREUND ADJUVANT; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PEPTIDE; TUMOR VACCINE;

EID: 0031758085     PISSN: 15249557     EISSN: 15374513     Source Type: Journal    
DOI: 10.1097/00002371-199811000-00001     Document Type: Article
Times cited : (32)

References (50)
  • 1
    • 0025175893 scopus 로고
    • Isolation and analysis of naturally processed viral peptides as recognized by cytotoxic T cells
    • Rötschke O, Falk K, Deres K, et al. Isolation and analysis of naturally processed viral peptides as recognized by cytotoxic T cells. Nature 1990;348:252-4.
    • (1990) Nature , vol.348 , pp. 252-254
    • Rötschke, O.1    Falk, K.2    Deres, K.3
  • 2
    • 0022483534 scopus 로고
    • The epitopes of influenza nucleoprotein recognized by cytotoxic T lymphocytes can be defined by short synthetic peptides
    • Townsend ARM, Rothbard J, Gotch FM, Bahadur G, Wraith D, McMichael AJ. The epitopes of influenza nucleoprotein recognized by cytotoxic T lymphocytes can be defined by short synthetic peptides. Cell 1986;44:959-68.
    • (1986) Cell , vol.44 , pp. 959-968
    • Townsend, A.R.M.1    Rothbard, J.2    Gotch, F.M.3    Bahadur, G.4    Wraith, D.5    McMichael, A.J.6
  • 3
    • 0025166228 scopus 로고
    • Isolation of an endogenously processed immunodominant viral peptide from the H-2Kb molecule
    • Van Bleek GM, Nathanson SG. Isolation of an endogenously processed immunodominant viral peptide from the H-2Kb molecule. Nature 1990;348:213-26.
    • (1990) Nature , vol.348 , pp. 213-226
    • Van Bleek, G.M.1    Nathanson, S.G.2
  • 4
    • 0028198644 scopus 로고
    • Peptide size selection by the major histocompatibility complex-encoded peptide transporter
    • Momburg F, Roelse J, Hämmerling GJ, Neefjes JJ. Peptide size selection by the major histocompatibility complex-encoded peptide transporter. J Exp Med 1994;179:1613-23.
    • (1994) J Exp Med , vol.179 , pp. 1613-1623
    • Momburg, F.1    Roelse, J.2    Hämmerling, G.J.3    Neefjes, J.J.4
  • 6
    • 0028098173 scopus 로고
    • Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator
    • Schumacher TNM, Kantesaria DV, Heemels M-T, et al. Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator. J Exp Med 1994;179:533-40.
    • (1994) J Exp Med , vol.179 , pp. 533-540
    • Schumacher, T.N.M.1    Kantesaria, D.V.2    Heemels, M.-T.3
  • 7
    • 0026318732 scopus 로고
    • The structure of the antigen-binding groove of MHC class I molecules determines specific selection of self peptides
    • Van Bleek GM, Nathanson SG. The structure of the antigen-binding groove of MHC class I molecules determines specific selection of self peptides. Proc Natl Acad Sci USA 1991; 88: 11032-6.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11032-11036
    • Van Bleek, G.M.1    Nathanson, S.G.2
  • 8
    • 0025155682 scopus 로고
    • Cellular peptide composition governed by major histocompatibility complex class I molecules
    • Falk K, Rotschke O, Rammensee HG. Cellular peptide composition governed by major histocompatibility complex class I molecules. Nature 1990;348:248-51.
    • (1990) Nature , vol.348 , pp. 248-251
    • Falk, K.1    Rotschke, O.2    Rammensee, H.G.3
  • 9
    • 0025855156 scopus 로고
    • Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
    • Falk K, Rotschke O, Stevanovic S, Jung G, Rammensee H-G. Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 1991;351:290-6.
    • (1991) Nature , vol.351 , pp. 290-296
    • Falk, K.1    Rotschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.-G.5
  • 10
    • 0026507564 scopus 로고
    • Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry
    • Hunt DF, Henderson RA, Shabanowitz J, et al. Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry. Science 1992;255:1261-3.
    • (1992) Science , vol.255 , pp. 1261-1263
    • Hunt, D.F.1    Henderson, R.A.2    Shabanowitz, J.3
  • 12
    • 0026673724 scopus 로고
    • Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb
    • Fremont DH, Matsumara M, Stura EA, Peterson PA, Wilson IA. Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb. Science 1992;257:919-27.
    • (1992) Science , vol.257 , pp. 919-927
    • Fremont, D.H.1    Matsumara, M.2    Stura, E.A.3    Peterson, P.A.4    Wilson, I.A.5
  • 13
    • 0026794581 scopus 로고
    • The threedimensional structure of HLA-B27 at 2.1 Â resolution suggests a general mechanism for tight peptide binding to MHC
    • Madden DR, Gorga JC, Strominger JL, Wiley DC. The threedimensional structure of HLA-B27 at 2.1 Â resolution suggests a general mechanism for tight peptide binding to MHC. Cell 1992; 70:1035-48.
    • (1992) Cell , vol.70 , pp. 1035-1048
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 14
    • 0026728457 scopus 로고
    • Emerging principle for the recognition of peptide antigens by MHC class I molecules
    • Matsumara M, Fremont DH, Peterson PA, Wilson IA. Emerging principle for the recognition of peptide antigens by MHC class I molecules. Science 1992;257:927-34.
    • (1992) Science , vol.257 , pp. 927-934
    • Matsumara, M.1    Fremont, D.H.2    Peterson, P.A.3    Wilson, I.A.4
  • 15
    • 0026713069 scopus 로고
    • Crystal structure of the MHC class I H-2Kb molecule containing a single viral peptide: Implications for peptide binding and T cell receptor recognition
    • Zhang W, Young ACM, Imarai M, Nathanson SC, Sachettini JC. Crystal structure of the MHC class I H-2Kb molecule containing a single viral peptide: implications for peptide binding and T cell receptor recognition. Proc Natl Acad Sci USA 1992;89:8403-7.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8403-8407
    • Zhang, W.1    Young, A.C.M.2    Imarai, M.3    Nathanson, S.C.4    Sachettini, J.C.5
  • 16
    • 0027304399 scopus 로고
    • Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules
    • Ruppert J, Sidney J, Cells E, Kubo RT, Grey HM, Sette A. Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules. Cell 1993;74:929-37.
    • (1993) Cell , vol.74 , pp. 929-937
    • Ruppert, J.1    Sidney, J.2    Cells, E.3    Kubo, R.T.4    Grey, H.M.5    Sette, A.6
  • 17
    • 0027211041 scopus 로고
    • Polymorphisms in pockets of MHC class I molecules influence peptide preference
    • Rohren EM, Pease LR, Pleogh HL, Schumacher TNM. Polymorphisms in pockets of MHC class I molecules influence peptide preference. J Exp Med 1993;177:1713-21.
    • (1993) J Exp Med , vol.177 , pp. 1713-1721
    • Rohren, E.M.1    Pease, L.R.2    Pleogh, H.L.3    Schumacher, T.N.M.4
  • 18
    • 0027210015 scopus 로고
    • Allele-specific B pocket transplant in class I MHC protein changes requirement for anchor residue at P2 of peptide
    • Colbert RA, Rowland-Jones SL, McMichael AJ, Frelinger JA. Allele-specific B pocket transplant in class I MHC protein changes requirement for anchor residue at P2 of peptide. Proc Natl Acad Sci USA 1993;90:6879-83.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6879-6883
    • Colbert, R.A.1    Rowland-Jones, S.L.2    McMichael, A.J.3    Frelinger, J.A.4
  • 19
    • 0025369192 scopus 로고
    • Peptide binding to HLA-DR1: A peptide with most residues substituted to alanine retains MHC binding
    • Jardetsky TS, Gorga JC, Busch R, Rothbard J, Strominger JL, Wiley DC. Peptide binding to HLA-DR1: a peptide with most residues substituted to alanine retains MHC binding. EMBO J 1990;9:1797-803.
    • (1990) EMBO J , vol.9 , pp. 1797-1803
    • Jardetsky, T.S.1    Gorga, J.C.2    Busch, R.3    Rothbard, J.4    Strominger, J.L.5    Wiley, D.C.6
  • 20
    • 0027173861 scopus 로고
    • Identification of peptide sequences that potentially trigger HLA-A2.1-restricted cytotoxic T lymphocytes
    • Nijman HW, Houbiers JGA, Vierboom MPM, et al. Identification of peptide sequences that potentially trigger HLA-A2.1-restricted cytotoxic T lymphocytes. Eur J Immunol 1993;23:1215-9.
    • (1993) Eur J Immunol , vol.23 , pp. 1215-1219
    • Nijman, H.W.1    Houbiers, J.G.A.2    Vierboom, M.P.M.3
  • 21
    • 0031053688 scopus 로고    scopus 로고
    • Analogues of CTL epitopes with improved MHC class I-binding capacity elicit anti-melanoma CTL recognizing the wild type epitope
    • Bakker ABH, van der Burg SH, Huijbens RJF, et al. Analogues of CTL epitopes with improved MHC class I-binding capacity elicit anti-melanoma CTL recognizing the wild type epitope. Int J Cancer 1997;70:302-9.
    • (1997) Int J Cancer , vol.70 , pp. 302-309
    • Bakker, A.B.H.1    van der Burg, S.H.2    Huijbens, R.J.F.3
  • 22
    • 0030587077 scopus 로고    scopus 로고
    • Improved induction of melanoma-reactive CTL with peptides from the melanoma antigen gplOO modified at HLA-A *0201-binding residues
    • Parkhurst MR, Salgaller ML, Southwood S, et al. Improved induction of melanoma-reactive CTL with peptides from the melanoma antigen gplOO modified at HLA-A *0201-binding residues. J Immunol 1996;157:2539-48.
    • (1996) J Immunol , vol.157 , pp. 2539-2548
    • Parkhurst, M.R.1    Salgaller, M.L.2    Southwood, S.3
  • 23
    • 0027320440 scopus 로고
    • Vaccination with cytotoxic T lymphocyte epitope-containing peptide protects against a tumor induced by human papillomavirus type 16-transformed cells
    • Feltkamp MCW, Smits HL, Vierboom MPM, et al. Vaccination with cytotoxic T lymphocyte epitope-containing peptide protects against a tumor induced by human papillomavirus type 16-transformed cells. Eur J Immunol 1993;23:2242-9.
    • (1993) Eur J Immunol , vol.23 , pp. 2242-2249
    • Feltkamp, M.C.W.1    Smits, H.L.2    Vierboom, M.P.M.3
  • 24
    • 0029143546 scopus 로고
    • CTL raised against a subdominant epitope offered as a synthetic peptide eradicate human papillomavirus type 16-induced tumors
    • Feltkamp MCW, Vreugdenhil GR, Vierboom MPM, et al. CTL raised against a subdominant epitope offered as a synthetic peptide eradicate human papillomavirus type 16-induced tumors. Eur J Immunol 1995;25:2638-42.
    • (1995) Eur J Immunol , vol.25 , pp. 2638-2642
    • Feltkamp, M.C.W.1    Vreugdenhil, G.R.2    Vierboom, M.P.M.3
  • 25
    • 0028125601 scopus 로고
    • Limitations of predictive motifs revealed by cytotoxic T lymphocyte epitope mapping of the human papillomavirus E7 protein
    • Sadnikova E, Zhu X, Collins S, et al. Limitations of predictive motifs revealed by cytotoxic T lymphocyte epitope mapping of the human papillomavirus E7 protein. Int Immunol 1994;6:289-96.
    • (1994) Int Immunol , vol.6 , pp. 289-296
    • Sadnikova, E.1    Zhu, X.2    Collins, S.3
  • 26
    • 0025999648 scopus 로고
    • Naturally-occurring peptide antigens derived from the MHC class-I restricted processing pathway
    • Rotschke O, Falk K. Naturally-occurring peptide antigens derived from the MHC class-I restricted processing pathway. Immunol Today 1991;12:447-55.
    • (1991) Immunol Today , vol.12 , pp. 447-455
    • Rotschke, O.1    Falk, K.2
  • 27
    • 0027974989 scopus 로고
    • The threedimensional structure of H-2Db at 2.4 A resolution: Implications for antigen-determinant selection
    • Young ACM, Zhang W, Sacchettini JC, Nathanson S. The threedimensional structure of H-2Db at 2.4 A resolution: implications for antigen-determinant selection. Cell 1994;76:39-50.
    • (1994) Cell , vol.76 , pp. 39-50
    • Young, A.C.M.1    Zhang, W.2    Sacchettini, J.C.3    Nathanson, S.4
  • 28
    • 0024466940 scopus 로고
    • Eradication of adenovirus El-induced tumors by ElA-specific cytotoxic T lymphocytes
    • Kast WM, Offringa R, Peters PJ, et al. Eradication of adenovirus El-induced tumors by ElA-specific cytotoxic T lymphocytes. Cell 1989;59:603-14.
    • (1989) Cell , vol.59 , pp. 603-614
    • Kast, W.M.1    Offringa, R.2    Peters, P.J.3
  • 29
    • 0000685691 scopus 로고
    • Studies in antibody response of mice to tumour inoculation
    • Gorer PA. Studies in antibody response of mice to tumour inoculation. Br J Cancer 1950;4:372-81.
    • (1950) Br J Cancer , vol.4 , pp. 372-381
    • Gorer, P.A.1
  • 30
    • 84988121049 scopus 로고
    • The RMA-S lymphoma mutant; consequences of a peptide loading defect on immunological recognition and graft rejection
    • Ljunggren H-G, Öhlen C, Höglund P, Franksson L, Kärre K. The RMA-S lymphoma mutant; consequences of a peptide loading defect on immunological recognition and graft rejection. Int J Cancer 1991; 6(suppl):38-44.
    • (1991) Int J Cancer , vol.6 , pp. 38-44
    • Ljunggren, H.-G.1    Öhlen, C.2    Höglund, P.3    Franksson, L.4    Kärre, K.5
  • 31
    • 84988087266 scopus 로고
    • Fine peptide specificity of cytotoxic T lymphocytes against adenovirus-induced tumours and peptide-MHC binding
    • Kast WM, Melief CJM. Fine peptide specificity of cytotoxic T lymphocytes against adenovirus-induced tumours and peptide-MHC binding. Int J Cancer 1991;6(suppl):90-4.
    • (1991) Int J Cancer , vol.6 , pp. 90-94
    • Kast, W.M.1    Melief, C.J.M.2
  • 32
    • 0027239749 scopus 로고
    • Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter
    • Neefjes JJ, Momburg F, Hämmerling GJ. Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter. Science 1993;261:769-71.
    • (1993) Science , vol.261 , pp. 769-771
    • Neefjes, J.J.1    Momburg, F.2    Hämmerling, G.J.3
  • 33
    • 0028829908 scopus 로고
    • Major differences in TAP-dependent translocation of MHC class I presentable peptides and the effect of flanking sequences
    • Neisig A, Roelse J, Sijts EJAM, et al. Major differences in TAP-dependent translocation of MHC class I presentable peptides and the effect of flanking sequences. J Immunol 1995;154:1273-9.
    • (1995) J Immunol , vol.154 , pp. 1273-1279
    • Neisig, A.1    Roelse, J.2    Sijts, E.J.A.M.3
  • 34
    • 0027074872 scopus 로고
    • Determination of cytotoxic T-lymphocyte precursor frequencies using europium labeling as a nonradioactive alternative to labeling with chromium-51
    • Bouma GJ, Van der Meer-Prins PMW, Van Bree FPMJ, Van Rood JJ, Claas FHJ. Determination of cytotoxic T-lymphocyte precursor frequencies using europium labeling as a nonradioactive alternative to labeling with chromium-51. Hum Immunol 1992;35:85-92.
    • (1992) Hum Immunol , vol.35 , pp. 85-92
    • Bouma, G.J.1    Van der Meer-Prins, P.M.W.2    Van Bree, F.P.M.J.3    Van Rood, J.J.4    Claas, F.H.J.5
  • 36
    • 0029146674 scopus 로고
    • Competition inhibition of cytotoxic T lymphocyte (CTL) lysis, a more sensitive method to identify candidate CTL epitopes than antibody-detected MHC class I stabilization
    • Feltkamp MCW, Vierboom MPM, Toes REM, et al. Competition inhibition of cytotoxic T lymphocyte (CTL) lysis, a more sensitive method to identify candidate CTL epitopes than antibody-detected MHC class I stabilization. Immunol Lett 1995;47:1-8.
    • (1995) Immunol Lett , vol.47 , pp. 1-8
    • Feltkamp, M.C.W.1    Vierboom, M.P.M.2    Toes, R.E.M.3
  • 37
    • 0028501143 scopus 로고
    • Efficiency of MHC class I antigen processing: A quantitative analysis
    • Villanueva MS, Fischer P, Feen K, Pamer EG. Efficiency of MHC class I antigen processing: a quantitative analysis. Immunity 1994; 1:479-89.
    • (1994) Immunity , vol.1 , pp. 479-489
    • Villanueva, M.S.1    Fischer, P.2    Feen, K.3    Pamer, E.G.4
  • 38
    • 0026482571 scopus 로고
    • Peptide-induced conformational changes in class I heavy chains alter MHC recognition
    • Bluestone JA, Jameson S, Miller S, Dick II R. Peptide-induced conformational changes in class I heavy chains alter MHC recognition. J Exp Med 1992;176:1757-61.
    • (1992) J Exp Med , vol.176 , pp. 1757-1761
    • Bluestone, J.A.1    Jameson, S.2    Miller, S.3    Dick, R.4
  • 40
    • 0028106321 scopus 로고
    • Peptide binding to the most frequent HLA-A alleles measured by quantitative molecular binding assays
    • Sette A, Sidney J, Del Guercio MF, et al. Peptide binding to the most frequent HLA-A alleles measured by quantitative molecular binding assays. Mol Immunol 1994;31:813-22.
    • (1994) Mol Immunol , vol.31 , pp. 813-822
    • Sette, A.1    Sidney, J.2    Del Guercio, M.F.3
  • 41
    • 0028077007 scopus 로고
    • Efficient MHC class I-peptide binding is required but does not ensure MHC class I-restricted immunogenicity
    • Feltkamp MCW, Vierboom MPM, Kast WM, Melief CJM. Efficient MHC class I-peptide binding is required but does not ensure MHC class I-restricted immunogenicity. Mol Immunol 1994; 31:1391-401.
    • (1994) Mol Immunol , vol.31 , pp. 1391-1401
    • Feltkamp, M.C.W.1    Vierboom, M.P.M.2    Kast, W.M.3    Melief, C.J.M.4
  • 42
    • 0028964889 scopus 로고
    • Peptide engineering allows T-cell vaccination against human papilloma virus tumour antigen, E6
    • Lipford GB, Bauer S, Wagner H, Heeg K. Peptide engineering allows T-cell vaccination against human papilloma virus tumour antigen, E6. Immunology 1995;84:298-303.
    • (1995) Immunology , vol.84 , pp. 298-303
    • Lipford, G.B.1    Bauer, S.2    Wagner, H.3    Heeg, K.4
  • 43
    • 0025886714 scopus 로고
    • Human papillomavirus in the pathogenesis of anogenital cancer
    • Zur Hausen H. Human papillomavirus in the pathogenesis of anogenital cancer. Virology 1991;184:9-13.
    • (1991) Virology , vol.184 , pp. 9-13
    • Zur Hausen, H.1
  • 44
    • 0025744619 scopus 로고
    • Nucleotide and amino acid sequence variation in the LI and E7 open reading frames of human papillomavirus type 6 and type 16
    • Icenogle JP, Sathya P, Miller DL, Tucker RA, Rawls WE. Nucleotide and amino acid sequence variation in the LI and E7 open reading frames of human papillomavirus type 6 and type 16. Virology 1991;184:101-7.
    • (1991) Virology , vol.184 , pp. 101-107
    • Icenogle, J.P.1    Sathya, P.2    Miller, D.L.3    Tucker, R.A.4    Rawls, W.E.5
  • 45
    • 0027442128 scopus 로고
    • The genetic drift of human papillomavirus type 16 is a means of reconstructing prehistoric viral spread and the movement of ancient populations
    • Ho L, Chan SY, Burk RD, et al. The genetic drift of human papillomavirus type 16 is a means of reconstructing prehistoric viral spread and the movement of ancient populations. J Virol 1993;67:6413-23.
    • (1993) J Virol , vol.67 , pp. 6413-6423
    • Ho, L.1    Chan, S.Y.2    Burk, R.D.3
  • 46
    • 0028104118 scopus 로고
    • Identification of a unique group of human papillomavirus type 16 sequence variants among clinical isolates from Barbados
    • Smits HL, Traanberg KF, Krul MRL, et al. Identification of a unique group of human papillomavirus type 16 sequence variants among clinical isolates from Barbados. J Gen Virol 1994;75: 2457-62.
    • (1994) J Gen Virol , vol.75 , pp. 2457-2462
    • Smits, H.L.1    Traanberg, K.F.2    Krul, M.R.L.3
  • 47
    • 0027977641 scopus 로고
    • An immunodominant MCF murine leukemia virus encoded CTL epitope, identified by its MHC class I-binding motif, explains MuLV type specificity of MCF-directed CTL
    • Sijts EJAM, Ossendorp F, Mengede EAM, Van den Elsen PJ, Melief CJM. An immunodominant MCF murine leukemia virus encoded CTL epitope, identified by its MHC class I-binding motif, explains MuLV type specificity of MCF-directed CTL. J Immunol 1994;152:106-16.
    • (1994) J Immunol , vol.152 , pp. 106-116
    • Sijts, E.J.A.M.1    Ossendorp, F.2    Mengede, E.A.M.3    Van den Elsen, P.J.4    Melief, C.J.M.5
  • 48
    • 0028261060 scopus 로고
    • Cytotoxic T-cell activity antagonized by naturally occurring HIV-1 gag variants
    • Klenerman P, Rowland-Jones S, McAdam S, et al. Cytotoxic T-cell activity antagonized by naturally occurring HIV-1 gag variants. Nature 1994;369:403-7.
    • (1994) Nature , vol.369 , pp. 403-407
    • Klenerman, P.1    Rowland-Jones, S.2    McAdam, S.3
  • 49
    • 0026503161 scopus 로고
    • Antigen analog-major histocompatibility complex act as antagonists of the T cell receptor
    • De Magristis MT, Alexander J, Coggeshall M, et al. Antigen analog-major histocompatibility complex act as antagonists of the T cell receptor. Cell 1992;68:625-34.
    • (1992) Cell , vol.68 , pp. 625-634
    • De Magristis, M.T.1    Alexander, J.2    Coggeshall, M.3
  • 50
    • 0028360076 scopus 로고
    • Natural variants of cytotoxic epitopes are T cell receptor antagonists for antiviral cytotoxic T cells
    • Bertoletti A, Sette A, Chisari FV, et al. Natural variants of cytotoxic epitopes are T cell receptor antagonists for antiviral cytotoxic T cells. Nature 1994;369:407-10.
    • (1994) Nature , vol.369 , pp. 407-410
    • Bertoletti, A.1    Sette, A.2    Chisari, F.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.