메뉴 건너뛰기




Volumn 287, Issue 22, 2012, Pages 18078-18090

Molecular recognition of Candida albicans (1→2)-β-mannan oligosaccharides by a protective monoclonal antibody reveals the immunodominance of internal saccharide residues

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY RECOGNITION; CANDIDA ALBICANS; CHEMICAL MAPPING; COMPUTATIONAL STUDIES; FRAMESHIFT; GLOBAL MINIMA; GLYCOCONJUGATE VACCINES; GLYCOCONJUGATES; HELICAL CONFORMATION; IMMUNODOMINANCE; IMMUNODOMINANT EPITOPES; LIGAND INTERACTIONS; MINIMAL LENGTHS; MOLECULAR RECOGNITION PATTERN; OBSERVATION POINT; POLYCLONAL; REDUCING ENDS; SATURATION TRANSFER; SELF-CONSISTENT MODEL; STRONG BINDING; TETRASACCHARIDES;

EID: 84861566843     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.355578     Document Type: Article
Times cited : (38)

References (52)
  • 1
    • 79957921817 scopus 로고    scopus 로고
    • Ashbee, H. R., and Bignell, E. M., Eds., Springer-Verlag, Berlin
    • MacCallum, D. M. (2010) In Pathogenic Yeasts, The Yeast Handbook, Ashbee, H. R., and Bignell, E. M., Eds., Springer-Verlag, Berlin, pp. 41-67
    • (2010) Pathogenic Yeasts, The Yeast Handbook , pp. 41-67
    • MacCallum, D.M.1
  • 2
    • 79551522540 scopus 로고    scopus 로고
    • Prospects for development of a vaccine to prevent and control vaginal candidiasis
    • Fidel, P. L., Jr., and Cutler, J. E. (2011) Prospects for development of a vaccine to prevent and control vaginal candidiasis. Curr. Infect. Dis. Rep. 13, 102-107
    • (2011) Curr. Infect. Dis. Rep. , vol.13 , pp. 102-107
    • Fidel Jr., P.L.1    Cutler, J.E.2
  • 3
    • 0346565461 scopus 로고    scopus 로고
    • Emerging issues in nosocomial fungal infections
    • Toscano, C. M., and Jarvis, W. R. (1999) Emerging issues in nosocomial fungal infections. Curr. Infect. Dis. Rep. 1, 347-361
    • (1999) Curr. Infect. Dis. Rep. , vol.1 , pp. 347-361
    • Toscano, C.M.1    Jarvis, W.R.2
  • 4
    • 34047269303 scopus 로고    scopus 로고
    • Advances in Topical and Systemic Antifungals
    • DOI 10.1016/j.det.2007.01.002, PII S0733863507000034, Drug Actions, Reactions, and Interactions
    • Zhang, A. Y., Camp, W. L., and Elewski, B. E. (2007) Advances in topical and systemic antifungals. Dermatol. Clin. 25, 165-183 (Pubitemid 46550722)
    • (2007) Dermatologic Clinics , vol.25 , Issue.2 , pp. 165-183
    • Zhang, A.Y.1    Camp, W.L.2    Elewski, B.E.3
  • 5
    • 33846518346 scopus 로고    scopus 로고
    • Candidiasi sistemiche neonatali
    • Stronati, M., and Decembrino, L. (2006) Neonatal invasive candidiasis. Minerva Pediatr. 58, 537-549 (Pubitemid 46156838)
    • (2006) Minerva Pediatrica , vol.58 , Issue.6 , pp. 537-549
    • Stronati, M.1    Decembrino, L.2
  • 6
    • 24144483474 scopus 로고    scopus 로고
    • Delaying the empiric treatment of Candida bloodstream infection until positive blood culture results are obtained: A potential risk factor for hospital mortality
    • DOI 10.1128/AAC.49.9.3640-3645.2005
    • Morrell, M., Fraser, V. J., and Kollef, M. H. (2005) Delaying the empiric treatment of Candida bloodstream infection until positive blood culture results are obtained. A potential risk factor for hospital mortality. Antimicrob. Agents Chemother. 49, 3640-3645 (Pubitemid 41233011)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.9 , pp. 3640-3645
    • Morrell, M.1    Fraser, V.J.2    Kollef, M.H.3
  • 7
    • 79957902458 scopus 로고    scopus 로고
    • The contribution of mouse models to our understanding of systemic candidiasis
    • Szabo, E. K., and MacCallum, D. M. (2011) The contribution of mouse models to our understanding of systemic candidiasis. FEMS Microbiol. Lett. 320, 1-8
    • (2011) FEMS Microbiol. Lett. , vol.320 , pp. 1-8
    • Szabo, E.K.1    MacCallum, D.M.2
  • 8
    • 20544435434 scopus 로고    scopus 로고
    • Defining criteria for anti-mannan antibodies to protect against candidiasis
    • Cutler, J. E. (2005) Defining criteria for anti-mannan antibodies to protect against candidiasis. Curr. Mol. Med. 5, 383-392
    • (2005) Curr. Mol. Med. , vol.5 , pp. 383-392
    • Cutler, J.E.1
  • 9
    • 0031796438 scopus 로고    scopus 로고
    • A vaccine and monoclonal antibodies that enhance mouse resistance to Candida albicans vaginal infection
    • Han, Y., Morrison, R. P., and Cutler, J. E. (1998)Avaccine and monoclonal antibodies that enhance mouse resistance to Candida albicans vaginal infection. Infect. Immun. 66, 5771-5776 (Pubitemid 28531833)
    • (1998) Infection and Immunity , vol.66 , Issue.12 , pp. 5771-5776
    • Han, Y.1    Morrison, R.P.2    Cutler, J.E.3
  • 10
    • 0029033902 scopus 로고
    • Antibody response that protects against disseminated candidiasis
    • Han, Y., and Cutler, J. E. (1995) Antibody response that protects against disseminated candidiasis. Infect. Immun. 63, 2714-2719
    • (1995) Infect. Immun. , vol.63 , pp. 2714-2719
    • Han, Y.1    Cutler, J.E.2
  • 11
    • 0032995552 scopus 로고    scopus 로고
    • Candida albicans mannan extract-protein conjugates induce a protective immune response against experimental candidiasis
    • DOI 10.1086/314779
    • Han, Y., Ulrich, M. A., and Cutler, J. E. (1999) Candida albicans mannan extract-protein conjugates induce a protective immune response against experimental candidiasis. J. Infect. Dis. 179, 1477-1484 (Pubitemid 29246598)
    • (1999) Journal of Infectious Diseases , vol.179 , Issue.6 , pp. 1477-1484
    • Han, Y.1    Ulrich, M.A.2    Cutler, J.E.3
  • 12
    • 35348873182 scopus 로고    scopus 로고
    • Synthesis and immunochemical studies on a Candida albicans cluster glycoconjugate vaccine
    • DOI 10.1039/b709912f
    • Wu, X., Lipinski, T., Carrel, F. R., Bailey, J. J., and Bundle, D. R. (2007) Synthesis and immunochemical studies on a Candida albicans cluster glycoconjugate vaccine. Org. Biomol. Chem. 5, 3477-3485 (Pubitemid 47587700)
    • (2007) Organic and Biomolecular Chemistry , vol.5 , Issue.21 , pp. 3477-3485
    • Wu, X.1    Lipinski, T.2    Carrel, F.R.3    Bailey, J.J.4    Bundle, D.R.5
  • 13
    • 51649093522 scopus 로고    scopus 로고
    • Synthetic glycopeptide vaccines combining β-mannan and peptide epitopes induce protection against candidiasis
    • Xin, H., Dziadek, S., Bundle, D. R., and Cutler, J. E. (2008) Synthetic glycopeptide vaccines combining β-mannan and peptide epitopes induce protection against candidiasis. Proc. Natl. Acad. Sci. U.S.A. 105, 13526-13531
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 13526-13531
    • Xin, H.1    Dziadek, S.2    Bundle, D.R.3    Cutler, J.E.4
  • 14
    • 0033983051 scopus 로고    scopus 로고
    • Protection against candidiasis by an immunoglobulin G3 (IgG3) monoclonal antibody specific for the same mannotriose as an IgM protective antibody
    • DOI 10.1128/IAI.68.3.1649-1654.2000
    • Han, Y., Riesselman, M. H., and Cutler, J. E. (2000) Protection against candidiasis by an immunoglobulin G3 (IgG3) monoclonal antibody specific for the same mannotriose as an IgM protective antibody. Infect. Immun. 68, 1649-1654 (Pubitemid 30108568)
    • (2000) Infection and Immunity , vol.68 , Issue.3 , pp. 1649-1654
    • Han, Y.1    Riesselman, M.H.2    Cutler, J.E.3
  • 15
    • 0036479303 scopus 로고    scopus 로고
    • The unique solution structure and immunochemistry of the Candida albicans β-1,2-mannopyranan cell wall antigens
    • DOI 10.1074/jbc.M109274200
    • Nitz, M., Ling, C. C., Otter, A., Cutler, J. E., and Bundle, D. R. (2002) The unique solution structure and immunochemistry of the Candida albicans β-1,2-mannopyranan cell wall antigens. J. Biol. Chem. 277, 3440-3446 (Pubitemid 34959966)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3440-3446
    • Nitz, M.1    Ling, C.-C.2    Otter, A.3    Cutler, J.E.4    Bundle, D.R.5
  • 16
    • 0024720498 scopus 로고
    • Structural study of phosphomannan of yeast-form cells of Candida albicans J-1012 strain with special reference to application of mild acetolysis
    • Kobayashi, H., Shibata, N., Mitobe, H., Ohkubo, Y., and Suzuki, S. (1989) Structural study of phosphomannan of yeast-form cells of Candida albicans J-1012 strain with special reference to application of mild acetolysis. Arch. Biochem. Biophys. 272, 364-375
    • (1989) Arch. Biochem. Biophys. , vol.272 , pp. 364-375
    • Kobayashi, H.1    Shibata, N.2    Mitobe, H.3    Ohkubo, Y.4    Suzuki, S.5
  • 18
    • 0026093891 scopus 로고
    • Structural study on a phosphorylated mannotetraose obtained from the phosphomannan of Candida albicans NIH B-792 strain by acetolysis
    • Shibata, N., Kobayashi, H., Takahashi, S., Okawa, Y., Hisamichi, K., and Suzuki, S. (1991) Structural study on a phosphorylated mannotetraose obtained from the phosphomannan of Candida albicans NIH B-792 strain by acetolysis. Arch. Biochem. Biophys. 290, 535-542
    • (1991) Arch. Biochem. Biophys. , vol.290 , pp. 535-542
    • Shibata, N.1    Kobayashi, H.2    Takahashi, S.3    Okawa, Y.4    Hisamichi, K.5    Suzuki, S.6
  • 19
    • 0022965642 scopus 로고
    • Characterization of phosphomannan-protein complexes isolated from viable cells of yeast and mycelial forms of Candida albicans NIH B-792 strain by the action of Zymolyase-100T
    • Shibata, N., Kobayashi, H., Tojo, M., and Suzuki, S. (1986) Characterization of phosphomannan-protein complexes isolated from viable cells of yeast and mycelial forms of Candida albicans NIH B-792 strain by the action of Zymolyase-100T. Arch. Biochem. Biophys. 251, 697-708
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 697-708
    • Shibata, N.1    Kobayashi, H.2    Tojo, M.3    Suzuki, S.4
  • 20
    • 0025439639 scopus 로고
    • Structure of the D-mannan of Candida stellatoidea IFO 1397 strain. Comparison with that of the phospho-D-mannan of Candida albicans NIH B-792 strain
    • Tojo, M., Shibata, N., Ban, Y., and Suzuki, S. (1990) Structure of the D-mannan of Candida stellatoidea IFO 1397 strain. Comparison with that of the phospho-D-mannan of Candida albicans NIH B-792 strain. Carbohydr. Res. 199, 215-226
    • (1990) Carbohydr. Res. , vol.199 , pp. 215-226
    • Tojo, M.1    Shibata, N.2    Ban, Y.3    Suzuki, S.4
  • 21
    • 34250695423 scopus 로고    scopus 로고
    • Chemical structure of the cell-wall mannan of Candida albicans serotype A and its difference in yeast and hyphal forms
    • DOI 10.1042/BJ20070081
    • Shibata, N., Suzuki, A., Kobayashi, H., and Okawa, Y. (2007) Chemical structure of the cell-wall mannan of Candida albicans serotype A and its difference in yeast and hyphal forms. Biochem. J 404, 365-372 (Pubitemid 46953910)
    • (2007) Biochemical Journal , vol.404 , Issue.3 , pp. 365-372
    • Shibata, N.1    Suzuki, A.2    Kobayashi, H.3    Okawa, Y.4
  • 22
    • 0030734676 scopus 로고    scopus 로고
    • Definitive chemical evidence for the constitutive ability of Candida albicans serotype A strains to synthesize β-1,2 linked oligomannosides containing up to 14 mannose residues
    • DOI 10.1016/S0014-5793(97)01205-2, PII S0014579397012052
    • Trinel, P. A., Lepage, G., Jouault, T., Strecker, G., and Poulain, D. (1997) Definitive chemical evidence for the constitutive ability of Candida albicans serotype A strains to synthesize β-1,2-linked oligomannosides containing up to 14 mannose residues. FEBS Lett. 416, 203-206 (Pubitemid 27462789)
    • (1997) FEBS Letters , vol.416 , Issue.2 , pp. 203-206
    • Trinel, P.A.1    Lepage, G.2    Jouault, T.3    Strecker, G.4    Poulain, D.5
  • 23
    • 4143145195 scopus 로고    scopus 로고
    • Candida albicans cell wall glycans, host receptors and responses: Elements for a decisive crosstalk
    • DOI 10.1016/j.mib.2004.06.011, PII S1369527404000773
    • Poulain, D., and Jouault, T. (2004) Candida albicans cell wall glycans, host receptors, and responses. Elements for a decisive crosstalk. Curr. Opin. Microbiol. 7, 342-349 (Pubitemid 39091117)
    • (2004) Current Opinion in Microbiology , vol.7 , Issue.4 , pp. 342-349
    • Poulain, D.1    Jouault, T.2
  • 24
    • 0002871105 scopus 로고
    • The upper limit for the size of the human antidextran combining site
    • Kabat, E. A. (1960) The upper limit for the size of the human antidextran combining site. J. Immunol. 84, 82-85
    • (1960) J. Immunol. , vol.84 , pp. 82-85
    • Kabat, E.A.1
  • 25
    • 0004285044 scopus 로고    scopus 로고
    • Hecht, S. M., ed. Oxford University Press, Oxford
    • Bundle, D. R. (1999) in Bioorganic Chemistry (Carbohydrates) (Hecht, S. M., ed.) pp. 370-440, Oxford University Press, Oxford
    • (1999) Bioorganic Chemistry (Carbohydrates) , pp. 370-440
    • Bundle, D.R.1
  • 26
    • 0022386258 scopus 로고
    • An immunochemical study of the combining site specificities of C57BL/6J monoclonal antibodies to α(1-6)-linked dextran B512
    • Newman, B. A., and Kabat, E. A. (1985) An immunochemical study of the combining site specificities of C57BL/6J monoclonal antibodies to α (1-6)-linked dextran B512. J. Immunol. 135, 1220-1231 (Pubitemid 16237440)
    • (1985) Journal of Immunology , vol.135 , Issue.2 , pp. 1220-1231
    • Newman, B.A.1    Kabat, E.A.2
  • 27
    • 84930583039 scopus 로고    scopus 로고
    • Kosma, P., and Müller-Loennies, S., eds Springer-Verlag, Wien, Austria
    • Jennings, H. J. (2012) in Anticarbohydrate Antibodies (Kosma, P., and Müller-Loennies, S., eds) pp. 55-74, Springer-Verlag, Wien, Austria
    • (2012) Anticarbohydrate Antibodies , pp. 55-74
    • Jennings, H.J.1
  • 29
    • 0035861619 scopus 로고    scopus 로고
    • Synthesis of di- to hexasaccharide 1,2-linked β-mannopyranan oligomers, a terminal S-linked tetrasaccharide congener and the corresponding BSA glycoconjugates
    • DOI 10.1021/jo010570x
    • Nitz, M., and Bundle, D. R. (2001) Synthesis of di- to hexasaccharide 1,2-linked β-mannopyranan oligomers, a terminal S-linked tetrasaccharide congener, and the corresponding BSA glycoconjugates. J. Org. Chem. 66, 8411-8423 (Pubitemid 34000639)
    • (2001) Journal of Organic Chemistry , vol.66 , Issue.25 , pp. 8411-8423
    • Nitz, M.1    Bundle, D.R.2
  • 30
    • 84905571820 scopus 로고    scopus 로고
    • A uniquely small, protective carbohydrate epitope may yield a conjugate vaccine for Candida albicans
    • Bundle, D. R., Nitz, M., Wu, X., and Sadowska, J. M. (2008) A uniquely small, protective carbohydrate epitope may yield a conjugate vaccine for Candida albicans. ACS Symp. Ser. 989, 163-183
    • (2008) ACS Symp. Ser. , vol.989 , pp. 163-183
    • Bundle, D.R.1    Nitz, M.2    Wu, X.3    Sadowska, J.M.4
  • 32
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • DOI 10.1002/(SICI)1521-3773(19990614)38:12<1784::AID-ANIE1784>3.0. CO;2-Q
    • Mayer, M., and Meyer, B. (1999) Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew. Chem. Int. Ed. 38, 1784-1788 (Pubitemid 29290947)
    • (1999) Angewandte Chemie - International Edition , vol.38 , Issue.12 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 33
    • 12444289530 scopus 로고    scopus 로고
    • 3 in native platelets than in liposomes
    • DOI 10.1021/ja044434w
    • Claasen, B., Axmann, M., Meinecke, R., and Meyer, B. (2005) Direct observation of ligand binding to membrane proteins in living cells by a saturation transfer double difference (STDD) NMR spectroscopy method shows a significantly higher affinity of integrin α(IIb)β3 in native platelets than in liposomes. J. Am. Chem. Soc. 127, 916-919 (Pubitemid 40144290)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.3 , pp. 916-919
    • Claasen, B.1    Axmann, M.2    Meinecke, R.3    Meyer, B.4
  • 34
    • 79960698472 scopus 로고
    • Water suppression that works. Excitation sculpting using arbitrary waveforms and pulsed field gradients
    • Hwang, T. L., and Shaka, A. J. (1995) Water suppression that works. Excitation sculpting using arbitrary waveforms and pulsed field gradients. J. Magn. Reson. Ser. A 112, 275-279
    • (1995) J. Magn. Reson. Ser. A , vol.112 , pp. 275-279
    • Hwang, T.L.1    Shaka, A.J.2
  • 35
    • 0030098150 scopus 로고    scopus 로고
    • Suppression of spin diffusion in selected frequency bands of nuclear Overhauser spectra
    • Vincent, S. J., Zwahlen, C., and Bodenhausen, G. (1996) Suppression of spin diffusion in selected frequency bands of nuclear Overhauser spectra. J. Biomol. NMR 7, 169-172 (Pubitemid 126709556)
    • (1996) Journal of Biomolecular NMR , vol.7 , Issue.2 , pp. 169-172
    • Vincent, S.J.F.1    Zwahlen, C.2    Bodenhausen, G.3
  • 36
    • 0033580680 scopus 로고    scopus 로고
    • NMR experiments reveal distinct antibody-bound conformations of a synthetic disaccharide representing a general structural element of bacterial lipopolysaccharide epitopes
    • Haselhorst, T., Espinosa, J. F., Jiménez-Barbero, J., Sokolowski, T., Kosma, P., Brade, H., Brade, L., and Peters, T. (1999) NMR experiments reveal distinct antibody-bound conformations of a synthetic disaccharide representing a general structural element of bacterial lipopolysaccharide epitopes. Biochemistry 38, 6449-6459
    • (1999) Biochemistry , vol.38 , pp. 6449-6459
    • Haselhorst, T.1    Espinosa, J.F.2    Jiménez-Barbero, J.3    Sokolowski, T.4    Kosma, P.5    Brade, H.6    Brade, L.7    Peters, T.8
  • 38
    • 0037110472 scopus 로고    scopus 로고
    • Effective Born radii in the generalized Born approximation: The importance of being perfect
    • DOI 10.1002/jcc.10126
    • Onufriev, A., Case, D. A., and Bashford, D. (2002) Effective born radii in the generalized born approximation. The importance of being perfect. J. Comput. Chem. 23, 1297-1304 (Pubitemid 35186231)
    • (2002) Journal of Computational Chemistry , vol.23 , Issue.14 , pp. 1297-1304
    • Onufriev, A.1    Case, D.A.2    Bashford, D.3
  • 39
    • 0034458999 scopus 로고    scopus 로고
    • WAM: An improved algorithm for modelling antibodies on the WEB
    • Whitelegg, N. R., and Rees, A. R. (2000)WAM. An improved algorithm for modeling antibodies on the WEB. Protein Eng. 13, 819-824 (Pubitemid 32233940)
    • (2000) Protein Engineering , vol.13 , Issue.12 , pp. 819-824
    • Whitelegg, N.R.J.1    Rees, A.R.2
  • 40
    • 0023769808 scopus 로고
    • Structure and energetics of ligand binding to proteins. Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system
    • Dauber-Osguthorpe, P., Roberts, V. A., Osguthorpe, D. J., Wolff, J., Genest, M., and Hagler, A. T. (1988) Structure and energetics of ligand binding to proteins. Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system. Proteins Struct. Funct. Genet. 4, 31-47
    • (1988) Proteins Struct. Funct. Genet. , vol.4 , pp. 31-47
    • Dauber-Osguthorpe, P.1    Roberts, V.A.2    Osguthorpe, D.J.3    Wolff, J.4    Genest, M.5    Hagler, A.T.6
  • 41
    • 0032540222 scopus 로고    scopus 로고
    • Assessing protein structures with a non-local atomic interaction energy
    • DOI 10.1006/jmbi.1998.1665
    • Melo, F., and Feytmans, E. (1998) Assessing protein structures with a non-local atomic interaction energy. J. Mol. Biol. 277, 1141-1152 (Pubitemid 28190852)
    • (1998) Journal of Molecular Biology , vol.277 , Issue.5 , pp. 1141-1152
    • Melo, F.1    Feytmans, E.2
  • 42
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D. Assessment of protein models with three-dimensional profiles
    • Eisenberg, D., Lüthy, R., and Bowie, J. U. (1997) VERIFY3D. Assessment of protein models with three-dimensional profiles. Methods Enzymol. 277, 396-404
    • (1997) Methods Enzymol. , vol.277 , pp. 396-404
    • Eisenberg, D.1    Lüthy, R.2    Bowie, J.U.3
  • 43
    • 0000243829 scopus 로고
    • PROCHECK. A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK. A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 44
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina. Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott, O., and Olson, A. J. (2010) AutoDock Vina. Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 31, 455-461
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 47
    • 84863715937 scopus 로고    scopus 로고
    • Synthesis of three trisaccharide congeners to investigate frame shifting of β-1,2-mannan homo-oligomers in an antibody binding site
    • in press
    • Costello, C., and Bundle, D. R. (2012) Synthesis of three trisaccharide congeners to investigate frame shifting of β-1,2-mannan homo-oligomers in an antibody binding site. Carbohydr. Res., in press
    • (2012) Carbohydr. Res.
    • Costello, C.1    Bundle, D.R.2
  • 48
    • 62549147093 scopus 로고    scopus 로고
    • Synthesis of monodeoxy and mono-O-methyl congeners of methyl β-D-mannopyranosyl-(1→2)-β-Dmannopyranoside for epitope mapping of anti-Candida albicans antibodies
    • Nycholat, C. M., and Bundle, D. R. (2009) Synthesis of monodeoxy and mono-O-methyl congeners of methyl β-D-mannopyranosyl-(1→2)-β- Dmannopyranoside for epitope mapping of anti-Candida albicans antibodies. Carbohydr. Res. 344, 1397-1411
    • (2009) Carbohydr. Res. , vol.344 , pp. 1397-1411
    • Nycholat, C.M.1    Bundle, D.R.2
  • 50
    • 0003129960 scopus 로고
    • Sela, M., ed Academic Press, Inc., New York
    • Jann, K., and Westphal, O. (1975) in The Antigens (Sela, M., ed) Vol. 3, pp. 1-125, Academic Press, Inc., New York
    • (1975) The Antigens , vol.3 , pp. 1-125
    • Jann, K.1    Westphal, O.2
  • 51
    • 84861567553 scopus 로고
    • Structure and immunological specificity of polysaccharides
    • Heidelberger, M. (1960) Structure and immunological specificity of polysaccharides. Fortsch. Chem. Org. Naturst. 18, 503-536
    • (1960) Fortsch. Chem. Org. Naturst. , vol.18 , pp. 503-536
    • Heidelberger, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.