메뉴 건너뛰기




Volumn 387, Issue 2, 2005, Pages 411-417

Peptide mimotopes of Mycobacterium tubercolosis carbohydrate immunodeterminants

Author keywords

Glycoconjugate; Immunodeterminant; Lipoarabinomannan (LAM); Mimotope; Mycobacterium; Phage display

Indexed keywords

ANTIBODIES; ANTIGENS; BACTERIA; BACTERIOPHAGES; CARBOHYDRATES; CELLS; DISEASES; IMMUNOLOGY;

EID: 17644384378     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041139     Document Type: Article
Times cited : (27)

References (28)
  • 1
    • 0031684282 scopus 로고    scopus 로고
    • Interactions between Mycobacterium tuberculosis and host cells: Are mycobacterial sugars the key?
    • Ehlers, M. R. W. and Daffé, M. (1998) Interactions between Mycobacterium tuberculosis and host cells: are mycobacterial sugars the key? Trends Microbiol. 6, 328-335
    • (1998) Trends Microbiol. , vol.6 , pp. 328-335
    • Ehlers, M.R.W.1    Daffé, M.2
  • 2
    • 0037844364 scopus 로고    scopus 로고
    • Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis
    • Brennan, P. J. (2003) Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis. Tuberculosis (Edinb.) 83, 91-97
    • (2003) Tuberculosis (Edinb.) , vol.83 , pp. 91-97
    • Brennan, P.J.1
  • 3
    • 0032452982 scopus 로고    scopus 로고
    • The envelope layers of mycobacteria with reference to their pathogenicity
    • Daffé, M. and Draper, P. (1998) The envelope layers of mycobacteria with reference to their pathogenicity. Adv. Microb. Physiol. 39, 131-203
    • (1998) Adv. Microb. Physiol. , vol.39 , pp. 131-203
    • Daffé, M.1    Draper, P.2
  • 6
    • 2342565753 scopus 로고    scopus 로고
    • Expression, secretion, and glycosylation of the 45- And 47-kDa glycoprotein of Mycobacterium tuberculosis in Streptomyces lividans
    • Lara, M., Servín González, L., Singh, M., Moreno, C., Cohen, I., Nimtz, M. and Espitia, C. (2004) Expression, secretion, and glycosylation of the 45- and 47-kDa glycoprotein of Mycobacterium tuberculosis in Streptomyces lividans. Appl. Environ. Microbiol. 70, 679-685
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 679-685
    • Lara, M.1    Servín González, L.2    Singh, M.3    Moreno, C.4    Cohen, I.5    Nimtz, M.6    Espitia, C.7
  • 7
    • 0028097922 scopus 로고
    • Structural features of the exocellular polysaccharides of Mycobacterium tuberculosis
    • Lemassu, A. and Daffé, M. (1994) Structural features of the exocellular polysaccharides of Mycobacterium tuberculosis. Biochem. J. 297, 351-357
    • (1994) Biochem. J. , vol.297 , pp. 351-357
    • Lemassu, A.1    Daffé, M.2
  • 8
    • 33947487166 scopus 로고
    • Gas-liquid chromatograptiy of trimethylsilyl derivatives of sugars and related substances
    • Sweeley, C. C., Bentley, R., Makita, M. and Wells, W. W. (1963) Gas-liquid chromatograptiy of trimethylsilyl derivatives of sugars and related substances. J. Am. Chem Soc. 85, 2497-2507
    • (1963) J. Am. Chem Soc. , vol.85 , pp. 2497-2507
    • Sweeley, C.C.1    Bentley, R.2    Makita, M.3    Wells, W.W.4
  • 10
    • 0000574356 scopus 로고
    • Small-scale preparation of single-stranded bacteriophage M13 DNA
    • (Sambrook, J., Fritsch, E. F. and Maniatis, T., eds.), Cold Spring Harbor Laboratory Press, Plainview, NY
    • Sambrook, J., Fritsch, E. F. and Maniatis, T. (1989) Small-scale preparation of single-stranded bacteriophage M13 DNA. In Molecular Cloning: A Laboratory Manual (Sambrook, J., Fritsch, E. F. and Maniatis, T., eds.), pp. 4.29-4.30, Cold Spring Harbor Laboratory Press, Plainview, NY
    • (1989) Molecular Cloning: A Laboratory Manual
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 13
    • 0029965091 scopus 로고    scopus 로고
    • Definition of the full extent of glycosylation of the 45-kilodalton glycoprotein of Mycobacterium tuberculosis
    • Dobos, K. M., Khoo, K. H., Swiderek, K. M., Brennan, P. J. and Belisle, J. T. (1996) Definition of the full extent of glycosylation of the 45-kilodalton glycoprotein of Mycobacterium tuberculosis. J. Bacteriol. 178, 2498-2506
    • (1996) J. Bacteriol. , vol.178 , pp. 2498-2506
    • Dobos, K.M.1    Khoo, K.H.2    Swiderek, K.M.3    Brennan, P.J.4    Belisle, J.T.5
  • 14
    • 0036774705 scopus 로고    scopus 로고
    • Characterization of the epitope of anti-lipoarabinomannan antibodies as the terminal hexaarabinofuranosyl motif of mycobacterial arabinans
    • Kaur, D., Lowary, T. L., Vissa, V. D., Crick, D. C. and Brennan, P. J. (2002) Characterization of the epitope of anti-lipoarabinomannan antibodies as the terminal hexaarabinofuranosyl motif of mycobacterial arabinans. Microbiology 148, 3049-3057
    • (2002) Microbiology , vol.148 , pp. 3049-3057
    • Kaur, D.1    Lowary, T.L.2    Vissa, V.D.3    Crick, D.C.4    Brennan, P.J.5
  • 15
    • 0038175124 scopus 로고    scopus 로고
    • Lipoarabinomannans:-from structure to biosynthesis
    • Nigou, J., Gilleron, M. and Puzo, G. (2003) Lipoarabinomannans:-from structure to biosynthesis. Biochimie 85, 153-166
    • (2003) Biochimie , vol.85 , pp. 153-166
    • Nigou, J.1    Gilleron, M.2    Puzo, G.3
  • 16
    • 0034717303 scopus 로고    scopus 로고
    • Structural and functional consequences of peptide-carbohydrate mimicry. Crystal structure of a carbohydrate-mimicking peptide bound to concanavalin A
    • Jain, D., Kaur, K., Sundaravadivel, B. and Salunke, D. M. (2000) Structural and functional consequences of peptide-carbohydrate mimicry. Crystal structure of a carbohydrate-mimicking peptide bound to concanavalin A. J. Biol. Chem. 275, 16098-16102
    • (2000) J. Biol. Chem. , vol.275 , pp. 16098-16102
    • Jain, D.1    Kaur, K.2    Sundaravadivel, B.3    Salunke, D.M.4
  • 18
    • 0035914380 scopus 로고    scopus 로고
    • Functional equality in the absence of structural similarity: An added dimension to molecular mimicry
    • Goel, M., Jain, D., Kaur, K. J., Kenoth, R., Maiya, B. G., Swamy, M. J. and Salunke, D. M. (2001) Functional equality in the absence of structural similarity: an added dimension to molecular mimicry. J. Biol. Chem. 276, 39277-39281
    • (2001) J. Biol. Chem. , vol.276 , pp. 39277-39281
    • Goel, M.1    Jain, D.2    Kaur, K.J.3    Kenoth, R.4    Maiya, B.G.5    Swamy, M.J.6    Salunke, D.M.7
  • 19
    • 0029974097 scopus 로고    scopus 로고
    • Monoclonal antibodies to surface antigens of Mycobacterium tuberculosis and their use in a modified enzyme-linked immunosorbent spot assay for detection of mycobacteria
    • Glatman-Freedman, A., Martin, J. M., Riska, P. F., Bloom, B. R. and Casadevall, A. (1996) Monoclonal antibodies to surface antigens of Mycobacterium tuberculosis and their use in a modified enzyme-linked immunosorbent spot assay for detection of mycobacteria. J. Clin. Microbiol. 34, 2795-2802
    • (1996) J. Clin. Microbiol. , vol.34 , pp. 2795-2802
    • Glatman-Freedman, A.1    Martin, J.M.2    Riska, P.F.3    Bloom, B.R.4    Casadevall, A.5
  • 23
    • 0033806584 scopus 로고    scopus 로고
    • Immunologic diagnosis of tuberculosis: A review
    • Chan, E. D., Heifets, L. and Iseman, R. D. (2000) Immunologic diagnosis of tuberculosis: a review. Tuber. Lung Dis. 80, 131-140
    • (2000) Tuber. Lung Dis. , vol.80 , pp. 131-140
    • Chan, E.D.1    Heifets, L.2    Iseman, R.D.3
  • 24
    • 0032757323 scopus 로고    scopus 로고
    • Deglycosylation of the 45/47-kilodalton antigen complex of Mycobacterium tuberculosis decreases its capacity to elicit in vivo or in vitro cellular immune responses
    • Romain, F., Horn, C., Pescher, P., Namane, A., Riviere, M., Puzo, G., Barzu, O. and Marchal, G. (1999) Deglycosylation of the 45/47-kilodalton antigen complex of Mycobacterium tuberculosis decreases its capacity to elicit in vivo or in vitro cellular immune responses. Infect. Immun. 67, 5567-5572
    • (1999) Infect. Immun. , vol.67 , pp. 5567-5572
    • Romain, F.1    Horn, C.2    Pescher, P.3    Namane, A.4    Riviere, M.5    Puzo, G.6    Barzu, O.7    Marchal, G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.