메뉴 건너뛰기




Volumn 151, Issue 7, 2005, Pages 2343-2351

Acd, a peptidoglycan hydrolase of Clostridium difficile with N-acetylglucosaminidase activity

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLGLUCOSAMINIDASE; AUTOLYSIN; BACTERIAL PROTEIN; CELL EXTRACT; HYDROLASE; MURAMIC ACID; N ACETYLGLUCOSAMINE; PEPTIDOGLYCAN; RECOMBINANT ENZYME;

EID: 22144486914     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.27878-0     Document Type: Article
Times cited : (29)

References (46)
  • 1
    • 0035192883 scopus 로고    scopus 로고
    • Electroporation of DNA sequences from the pathogenicity locus (PaLoc) of toxigenic Clostridium difficile into a non-toxigenic strain
    • Ackermann, G., Tang, Y. J., Henderson, J. P., Rodloff, A. C., Silva, J., Jr & Cohen, S. H. (2001). Electroporation of DNA sequences from the pathogenicity locus (PaLoc) of toxigenic Clostridium difficile into a non-toxigenic strain. Mol Cell Probes 15, 301-306.
    • (2001) Mol. Cell Probes , vol.15 , pp. 301-306
    • Ackermann, G.1    Tang, Y.J.2    Henderson, J.P.3    Rodloff, A.C.4    Silva Jr., J.5    Cohen, S.H.6
  • 2
    • 0035142066 scopus 로고    scopus 로고
    • Staphylococcus caprae strains carry determinants known to be involved in pathogenicity: A gene encoding an autolysin-binding fibronectin and the ica operon involved in biofilm formation
    • Allignet, J., Aubert, S., Dyke, K. G. & El Solh, N. (2001). Staphylococcus caprae strains carry determinants known to be involved in pathogenicity: a gene encoding an autolysin-binding fibronectin and the ica operon involved in biofilm formation. Infect Immun 69, 712-718.
    • (2001) Infect. Immun. , vol.69 , pp. 712-718
    • Allignet, J.1    Aubert, S.2    Dyke, K.G.3    El Solh, N.4
  • 3
    • 0037031133 scopus 로고    scopus 로고
    • Several regions of the repeat domain of the Staphylococcus caprae autolysin, AtlC, are involved in fibronectin binding
    • Allignet, J., England, P., Old, I. & El Solh, N. (2002). Several regions of the repeat domain of the Staphylococcus caprae autolysin, AtlC, are involved in fibronectin binding. FEMS Microbiol Lett 213, 193-197.
    • (2002) FEMS Microbiol. Lett. , vol.213 , pp. 193-197
    • Allignet, J.1    England, P.2    Old, I.3    El Solh, N.4
  • 4
    • 0032985757 scopus 로고    scopus 로고
    • Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP 5 in peptidoglycan maturation
    • Atrih, A., Bacher, G., Allmaier, G., Williamson, M. P. & Foster, S. J. (1999). Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP 5 in peptidoglycan maturation. J Bacteriol 181, 3956-3966.
    • (1999) J. Bacteriol. , vol.181 , pp. 3956-3966
    • Atrih, A.1    Bacher, G.2    Allmaier, G.3    Williamson, M.P.4    Foster, S.J.5
  • 5
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)
    • Bateman, A. & Bycroft, M. (2000). The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J Mol Biol 299, 1113-1119.
    • (2000) J. Mol. Biol. , vol.299 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 6
    • 0030608784 scopus 로고    scopus 로고
    • InlB: An invasion protein of Listeria monocytogenes with a novel type of surface association
    • Braun, L., Dramsi, S., Dehoux, P., Bierne, H., Lindahl, G. & Cossart, P. (1997). InlB: an invasion protein of Listeria monocytogenes with a novel type of surface association. Mol Microbiol 25, 285-294.
    • (1997) Mol. Microbiol. , vol.25 , pp. 285-294
    • Braun, L.1    Dramsi, S.2    Dehoux, P.3    Bierne, H.4    Lindahl, G.5    Cossart, P.6
  • 7
    • 0028907622 scopus 로고
    • Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation
    • Buist, G., Kok, J., Leenhouts, K. J., Dabrowska, M., Venema, G. & Haandrikman, A. J. (1995). Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation. J Bacteriol 177, 1554-1563.
    • (1995) J. Bacteriol. , vol.177 , pp. 1554-1563
    • Buist, G.1    Kok, J.2    Leenhouts, K.J.3    Dabrowska, M.4    Venema, G.5    Haandrikman, A.J.6
  • 8
  • 9
    • 0029016207 scopus 로고
    • The role of pneumolysin and autolysin in the pathology of pneumonia and septicemia in mice infected with a type 2 pneumococcus
    • Canvin, J. R., Marvin, A. P., Sivakumaran, M., Paton, J. C., Boulnois, G. J., Andrew, P. W. & Mitchell, T. J. (1995). The role of pneumolysin and autolysin in the pathology of pneumonia and septicemia in mice infected with a type 2 pneumococcus. J Infect Dis 172, 119-123.
    • (1995) J. Infect. Dis. , vol.172 , pp. 119-123
    • Canvin, J.R.1    Marvin, A.P.2    Sivakumaran, M.3    Paton, J.C.4    Boulnois, G.J.5    Andrew, P.W.6    Mitchell, T.J.7
  • 10
    • 0344393481 scopus 로고    scopus 로고
    • Identification and characterization of a peptidoglycan hydrolase, MurA, of Listeria monocytogenes, a muramidase needed for cell separation
    • Carroll, S. A., Hain, T., Technow, U., Darji, A., Pashalidis, P., Joseph, S. W. & Chakraborty, T. (2003). Identification and characterization of a peptidoglycan hydrolase, MurA, of Listeria monocytogenes, a muramidase needed for cell separation. J Bacteriol 185, 6801-6808.
    • (2003) J. Bacteriol. , vol.185 , pp. 6801-6808
    • Carroll, S.A.1    Hain, T.2    Technow, U.3    Darji, A.4    Pashalidis, P.5    Joseph, S.W.6    Chakraborty, T.7
  • 11
    • 0030924599 scopus 로고    scopus 로고
    • Molecular characterization of a germination-specific muramidase from Clostridium perfringens S40 spores and nucleotide sequence of the corresponding gene
    • Chen, Y., Miyata, S., Makino, S. & Moriyama, R. (1997). Molecular characterization of a germination-specific muramidase from Clostridium perfringens S40 spores and nucleotide sequence of the corresponding gene. J Bacteriol 179, 3181-3187.
    • (1997) J. Bacteriol. , vol.179 , pp. 3181-3187
    • Chen, Y.1    Miyata, S.2    Makino, S.3    Moriyama, R.4
  • 12
    • 2142808787 scopus 로고    scopus 로고
    • A comparative genome analysis identifies distinct sorting pathways in gram-positive bacteria
    • Comfort, D. & Clubb, R. T. (2004). A comparative genome analysis identifies distinct sorting pathways in gram-positive bacteria. Infect Immun 72, 2710-2722.
    • (2004) Infect. Immun. , vol.72 , pp. 2710-2722
    • Comfort, D.1    Clubb, R.T.2
  • 13
    • 0037368020 scopus 로고    scopus 로고
    • Genotypic differentiation of twelve Clostridium species by polymorphism analysis of the triosephosphate isomerase (tpi) gene
    • Dhalluin, A., Lemée, L., Pestel-Caron, M., Mory, F., Leluan, G., Lemeland, J. F. & Pons, J. L. (2003). Genotypic differentiation of twelve Clostridium species by polymorphism analysis of the triosephosphate isomerase (tpi) gene. Syst Appl Microbiol 26, 90-96.
    • (2003) Syst. Appl. Microbiol. , vol.26 , pp. 90-96
    • Dhalluin, A.1    Lemée, L.2    Pestel-Caron, M.3    Mory, F.4    Leluan, G.5    Lemeland, J.F.6    Pons, J.L.7
  • 14
    • 0026786136 scopus 로고
    • Role of the major pneumococcal autolysin in the atypical response of a clinical isolate of Streptococcus pneumoniae
    • Diaz, E., Lopez, R. & Garcia, J. L. (1992). Role of the major pneumococcal autolysin in the atypical response of a clinical isolate of Streptococcus pneumoniae. J Bacteriol 174, 5508-5515.
    • (1992) J. Bacteriol. , vol.174 , pp. 5508-5515
    • Diaz, E.1    Lopez, R.2    Garcia, J.L.3
  • 15
    • 0025077034 scopus 로고
    • Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci
    • Fischetti, V. A., Pancholi, V. & Schneewind, O. (1990). Conservation of a hexapeptide sequence in the anchor region of surface proteins from gram-positive cocci. Mol Microbiol 4, 1603-1605.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1603-1605
    • Fischetti, V.A.1    Pancholi, V.2    Schneewind, O.3
  • 16
    • 0025779454 scopus 로고
    • Cloning, expression, sequence analysis and biochemical characterization of an autolytic amidase of Bacillus subtilis 168 trpC2
    • Foster, S. J. (1991). Cloning, expression, sequence analysis and biochemical characterization of an autolytic amidase of Bacillus subtilis 168 trpC2. J Gen Microbiol 137, 1987-1998.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 1987-1998
    • Foster, S.J.1
  • 17
    • 0021402529 scopus 로고
    • Antimicrobial agent associated colitis and diarrhea: Historical background and clinical aspects
    • George, W. L. (1984). Antimicrobial agent associated colitis and diarrhea: historical background and clinical aspects. Rev Infect Dis 6, 208-213.
    • (1984) Rev. Infect. Dis. , vol.6 , pp. 208-213
    • George, W.L.1
  • 19
    • 0034065895 scopus 로고    scopus 로고
    • The Staphylococcus aureus lrgAB operon modulates murein hydrolase activity and penicillin tolerance
    • Groicher, K. H., Firek, B. A., Fujimoto, D. F. & Bayles, K. W. (2000). The Staphylococcus aureus lrgAB operon modulates murein hydrolase activity and penicillin tolerance. J Bacteriol 182, 1794-1801.
    • (2000) J. Bacteriol. , vol.182 , pp. 1794-1801
    • Groicher, K.H.1    Firek, B.A.2    Fujimoto, D.F.3    Bayles, K.W.4
  • 20
    • 0030798156 scopus 로고    scopus 로고
    • Evidence for autolysin-mediated primary attachment of Staphylococcus epidermidis to a polystyrene surface
    • Heilmann, C., Hussain, M., Peters, G. & Gotz, F. (1997). Evidence for autolysin-mediated primary attachment of Staphylococcus epidermidis to a polystyrene surface. Mol Microbiol 24, 1013-1024.
    • (1997) Mol. Microbiol. , vol.24 , pp. 1013-1024
    • Heilmann, C.1    Hussain, M.2    Peters, G.3    Gotz, F.4
  • 21
    • 0031904826 scopus 로고    scopus 로고
    • Cloning of aas, a gene encoding a Staphylococcus saprophyticus surface protein with adhesive and autolytic properties
    • Hell, W., Meyer, H. G. & Gatermann, S. G. (1998). Cloning of aas, a gene encoding a Staphylococcus saprophyticus surface protein with adhesive and autolytic properties. Mol Microbiol 29, 871-881.
    • (1998) Mol. Microbiol. , vol.29 , pp. 871-881
    • Hell, W.1    Meyer, H.G.2    Gatermann, S.G.3
  • 22
    • 0037457806 scopus 로고    scopus 로고
    • LytG of Bacillus subtilis is a novel peptidoglycan hydrolase: The major active glucosaminidase
    • Horsburgh, G. J., Atrih, A., Williamson, M. P. & Foster, S. J. (2003). LytG of Bacillus subtilis is a novel peptidoglycan hydrolase: the major active glucosaminidase. Biochemistry 42, 257-264.
    • (2003) Biochemistry , vol.42 , pp. 257-264
    • Horsburgh, G.J.1    Atrih, A.2    Williamson, M.P.3    Foster, S.J.4
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0024470531 scopus 로고
    • Detection of bacterial cell wall hydrolases after denaturing polyacrylamide gel electrophoresis
    • Leclerc, D. & Asselin, A. (1989). Detection of bacterial cell wall hydrolases after denaturing polyacrylamide gel electrophoresis. Can J Microbiol 35, 749-753.
    • (1989) Can. J. Microbiol. , vol.35 , pp. 749-753
    • Leclerc, D.1    Asselin, A.2
  • 26
    • 2942594170 scopus 로고    scopus 로고
    • Multilocus sequence typing analysis of human and animal Clostridium difficile isolates of various toxigenic types
    • Lemée, L., Dhalluin, A., Pestel-Caron, M., Lemeland, J. F. & Pons, J. L. (2004a). Multilocus sequence typing analysis of human and animal Clostridium difficile isolates of various toxigenic types. J Clin Microbiol 42, 2609-2617.
    • (2004) J. Clin. Microbiol. , vol.42 , pp. 2609-2617
    • Lemée, L.1    Dhalluin, A.2    Pestel-Caron, M.3    Lemeland, J.F.4    Pons, J.L.5
  • 27
    • 10844293286 scopus 로고    scopus 로고
    • Multiplex PCR targeting tpi (triosephosphate isomerase), tcdA (toxin A) and tcdB (toxin B) genes for toxigenic culture of C. difficile
    • Lemée, L., Dhalluin, A., Testelin, S., Mattrat M. A., Maillard, K., Lemeland, J. F. & Pons, J. L. (2004b). Multiplex PCR targeting tpi (triosephosphate isomerase), tcdA (toxin A) and tcdB (toxin B) genes for toxigenic culture of C. difficile. J Clin Microbiol 42, 5710-5714.
    • (2004) J. Clin. Microbiol. , vol.42 , pp. 5710-5714
    • Lemée, L.1    Dhalluin, A.2    Testelin, S.3    Mattrat, M.A.4    Maillard, K.5    Lemeland, J.F.6    Pons, J.L.7
  • 28
    • 0142091351 scopus 로고    scopus 로고
    • SecA2-dependent secretion of autolytic enzymes promotes Listeria monocytogenes pathogenesis
    • Lenz, L. L., Mohammadi, S., Geissler, A. & Portnoy, D. A. (2003). SecA2-dependent secretion of autolytic enzymes promotes Listeria monocytogenes pathogenesis. Proc Natl Acad Sci U S A 100, 12432-12437.
    • (2003) Proc. Natl. Acad. Sci. U S A , vol.100 , pp. 12432-12437
    • Lenz, L.L.1    Mohammadi, S.2    Geissler, A.3    Portnoy, D.A.4
  • 29
    • 0035350814 scopus 로고    scopus 로고
    • Clostridium beijerinckii and Clostridium difficile detoxify methyl-glyoxal by a novel mechanism involving glycerol dehydrogenase
    • Liyanage, H., Kashket S., Young, M. & Kashket, E. R. (2001). Clostridium beijerinckii and Clostridium difficile detoxify methyl-glyoxal by a novel mechanism involving glycerol dehydrogenase. Appl Environ Microbiol 67, 2004-2010.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2004-2010
    • Liyanage, H.1    Kashket, S.2    Young, M.3    Kashket, E.R.4
  • 31
    • 0035103227 scopus 로고    scopus 로고
    • The autolysin Ami contributes to the adhesion of Listeria monocytogenes to eukaryotic cells via its cell wall anchor
    • Milohanic, E., Jonquieres, R., Cossart, P., Berche, P. & Gaillard, J. L. (2001). The autolysin Ami contributes to the adhesion of Listeria monocytogenes to eukaryotic cells via its cell wall anchor. Mol Microbiol 39, 1212-1224.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1212-1224
    • Milohanic, E.1    Jonquieres, R.2    Cossart, P.3    Berche, P.4    Gaillard, J.L.5
  • 32
    • 0028865562 scopus 로고
    • A gene (sleC) encoding a spore-cortex-lytic enzyme from Clostridium perfringens S40 spores; cloning, sequence analysis and molecular characterization
    • Miyata, S., Moriyama, R., Miyahara, N. & Makino, S. (1995). A gene (sleC) encoding a spore-cortex-lytic enzyme from Clostridium perfringens S40 spores; cloning, sequence analysis and molecular characterization. Microbiology 141, 2643-2650.
    • (1995) Microbiology , vol.141 , pp. 2643-2650
    • Miyata, S.1    Moriyama, R.2    Miyahara, N.3    Makino, S.4
  • 33
    • 0025017621 scopus 로고
    • Two bactericidal targets for penicillin in pneumococci: Autolysis-dependent and autolysis-independent killing mechanisms
    • Moreillon, P., Markiewicz, Z., Nachman, S. & Tomasz, A. (1990). Two bactericidal targets for penicillin in pneumococci: autolysis-dependent and autolysis-independent killing mechanisms. Antimicrob Agents Chemother 34, 33-39.
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 33-39
    • Moreillon, P.1    Markiewicz, Z.2    Nachman, S.3    Tomasz, A.4
  • 34
    • 0028298861 scopus 로고
    • Gene cloning in Clostridium difficile using Tn916 as a shuttle conjugative transposon
    • Mullany, P., Wilks, M., Puckey, L. & Tabaqchali, S. (1994). Gene cloning in Clostridium difficile using Tn916 as a shuttle conjugative transposon. Plasmid 31, 320-323.
    • (1994) Plasmid , vol.31 , pp. 320-323
    • Mullany, P.1    Wilks, M.2    Puckey, L.3    Tabaqchali, S.4
  • 36
    • 0028908856 scopus 로고
    • Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-β-N-acetylglucosaminidase domain: Cloning, sequence analysis, and characterization
    • Oshida, T., Sugai, M., Komatsuzawa, H., Hong, Y. M., Suginaka, H. & Tomasz, A. (1995). A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-β-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization. Proc Natl Acad Sci U S A 92, 285-289.
    • (1995) Proc. Natl. Acad. Sci. U S A , vol.92 , pp. 285-289
    • Oshida, T.1    Sugai, M.2    Komatsuzawa, H.3    Hong, Y.M.4    Suginaka, H.5    Tomasz, A.A.6
  • 37
    • 0036430107 scopus 로고    scopus 로고
    • Conjugative transfer of clostridial shuttle vectors from Escherichia coli to Clostridium difficile through circumvention of the restriction barrier
    • Purdy, D., O'Keeffe, T. A., Elmore, M., Herbert, M., McLeod, A., Bokori-Brown, M., Ostrowski, A. & Minton, N. P. (2002). Conjugative transfer of clostridial shuttle vectors from Escherichia coli to Clostridium difficile through circumvention of the restriction barrier. Mol Microbiol 46, 439-452.
    • (2002) Mol. Microbiol. , vol.46 , pp. 439-452
    • Purdy, D.1    O'Keeffe, T.A.2    Elmore, M.3    Herbert, M.4    McLeod, A.5    Bokori-Brown, M.6    Ostrowski, A.7    Minton, N.P.8
  • 38
    • 0028805257 scopus 로고
    • Glucosaminidase of Bacillus subtilis: Cloning, regulation, primary structure and biochemical characterization
    • Rashid, M. H., Mori, M. & Sekiguchi, J. (1995). Glucosaminidase of Bacillus subtilis: cloning, regulation, primary structure and biochemical characterization. Microbiology 141, 2391-2404.
    • (1995) Microbiology , vol.141 , pp. 2391-2404
    • Rashid, M.H.1    Mori, M.2    Sekiguchi, J.3
  • 40
    • 77956866741 scopus 로고
    • Microbial peptidoglycan (murein) hydrolases
    • Edited by J.-M. Ghuysen & R. Hakenbeck. Amsterdam: Elsevier
    • Shockman, G. D. & Holtje, J.-V. (1994). Microbial peptidoglycan (murein) hydrolases. In Bacterial Cell Wall, pp. 131-166. Edited by J.-M. Ghuysen & R. Hakenbeck. Amsterdam: Elsevier.
    • (1994) Bacterial Cell Wall , pp. 131-166
    • Shockman, G.D.1    Holtje, J.-V.2
  • 41
    • 0033950951 scopus 로고    scopus 로고
    • Autolysins of Bacillus subtilis: Multiple enzymes with multiple functions
    • Smith, T. J., Blackman, S. A. & Foster, S. J. (2000). Autolysins of Bacillus subtilis: multiple enzymes with multiple functions. Microbiology 146, 249-262.
    • (2000) Microbiology , vol.146 , pp. 249-262
    • Smith, T.J.1    Blackman, S.A.2    Foster, S.J.3
  • 42
    • 0034960958 scopus 로고    scopus 로고
    • Evidence for holin function of tcdE gene in the pathogenicity of Clostridium difficile
    • Tan, K. S., Wee, B. Y. & Song, K. P. (2001). Evidence for holin function of tcdE gene in the pathogenicity of Clostridium difficile. J Med Microbiol 50, 613-619.
    • (2001) J. Med. Microbiol. , vol.50 , pp. 613-619
    • Tan, K.S.1    Wee, B.Y.2    Song, K.P.3
  • 43
    • 2942561968 scopus 로고    scopus 로고
    • Proteomics of protein secretion by Bacillus subtilis: Separating the 'secrets' of the secretome
    • 11 other authors
    • Tjalsma, H., Antelmann, H., Jongbloed, J. D. & 11 other authors (2004). Proteomics of protein secretion by Bacillus subtilis: separating the 'secrets' of the secretome. Microbiol Mol Biol Rev 68, 207-233.
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 207-233
    • Tjalsma, H.1    Antelmann, H.2    Jongbloed, J.D.3
  • 44
    • 0038039670 scopus 로고    scopus 로고
    • The staphylococcal cell wall
    • Edited by V. A. Fischetti. Washington, DC: American Society for Microbiology
    • Tomasz, A. (2000). The staphylococcal cell wall. In Gram-Positive Pathogens, pp. 351-360. Edited by V. A. Fischetti. Washington, DC: American Society for Microbiology.
    • (2000) Gram-Positive Pathogens , pp. 351-360
    • Tomasz, A.1
  • 45
    • 0002066459 scopus 로고
    • Bacterial autolysins: Specificity and function
    • Edited by C. Nombela. Amsterdam: Elsevier
    • Ward, J. B. & Williamson, R. (1984). Bacterial autolysins: specificity and function. In Microbial Cell Wall Synthesis and Autolysis, pp. 159-166. Edited by C. Nombela. Amsterdam: Elsevier.
    • (1984) Microbial Cell Wall Synthesis and Autolysis , pp. 159-166
    • Ward, J.B.1    Williamson, R.2
  • 46
    • 0025896984 scopus 로고
    • A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences
    • Wren, B. W. (1991). A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences. Mol Microbiol 5, 797-803.
    • (1991) Mol. Microbiol. , vol.5 , pp. 797-803
    • Wren, B.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.