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Volumn 150, Issue 5, 2011, Pages 545-552

Engineering of the glycan-binding specificity of Agrocybe cylindracea galectin towards α(2,3)-linked sialic acid by saturation mutagenesis

Author keywords

Agrocybe cylindracea galectin; frontal affinity chromatography; hydrogen bond; saturation mutagenesis; sialo binding lectin

Indexed keywords

ALPHA(2,3) SIALIC ACID; ASPARAGINE; GALECTIN; GLUCOSE; GLUTAMIC ACID; LACTOSE; OLIGOSACCHARIDE; SIALIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 80455156051     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvr094     Document Type: Article
Times cited : (29)

References (38)
  • 1
    • 0025316193 scopus 로고
    • Sialic acid binding lectins
    • Mandal, C. and Mandal, C. (1990) Sialic acid binding lectins. Experientia 46, 433-441
    • (1990) Experientia , vol.46 , pp. 433-441
    • Mandal, C.1    Mandal, C.2
  • 2
    • 0026920652 scopus 로고
    • Sialic acid-binding proteins: Characterization biological function and application
    • Zeng, F.Y. and Gabius, H.J. (1992) Sialic acid-binding proteins: Characterization, biological function and application. Z. Naturforsch. 47c, 641-653
    • (1992) Z. Naturforsch. , vol.47 , pp. 641-653
    • Zeng, F.Y.1    Gabius, H.J.2
  • 3
    • 33745309867 scopus 로고    scopus 로고
    • Sialic acid-specific lectins: Occurrence, specificity and function
    • Lehmann, F., Tiralongo, E., and Tiralongo, J. (2006) Sialic acid-specific lectins: Occurrence, specificity and function. Cell Mol. Life Sci. 63, 1331-1354
    • (2006) Cell Mol. Life Sci. , vol.63 , pp. 1331-1354
    • Lehmann, F.1    Tiralongo, E.2    Tiralongo, J.3
  • 4
    • 0038182574 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function
    • Michele, D.E. and Campbell, K.P. (2003) Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function. J. Biol. Chem. 278, 15457-15460
    • (2003) J. Biol. Chem. , vol.278 , pp. 15457-15460
    • Michele, D.E.1    Campbell, K.P.2
  • 6
    • 40949111464 scopus 로고    scopus 로고
    • Tissue and serum a2-3- and a2-6-linkage specific sialylation changes in oral carcinogenesis
    • Shah, M.H., Telang, S.D., Shah, P.M., and Patel, P.S. (2008) Tissue and serum a2-3- and a2-6-linkage specific sialylation changes in oral carcinogenesis. Glycoconj. J. 25, 279-290
    • (2008) Glycoconj. J. , vol.25 , pp. 279-290
    • Shah, M.H.1    Telang, S.D.2    Shah, P.M.3    Patel, P.S.4
  • 7
    • 67349241923 scopus 로고    scopus 로고
    • High expression of a a2,3-linked sialic acid residues is associated with the metastatic potential of human gastric cancer
    • Wang, F.L., Cui, S.X., Sun, L.P., Qu, X.J., Xie, Y.Y., Zhou, L., Mu, Y.L., Tang, W., and Wang, Y.S. (2009) High expression of a a2,3-linked sialic acid residues is associated with the metastatic potential of human gastric cancer. Cancer Detect. Prev. 32, 437-443
    • (2009) Cancer Detect. Prev. , vol.32 , pp. 437-443
    • Wang, F.L.1    Cui, S.X.2    Sun, L.P.3    Qu, X.J.4    Xie, Y.Y.5    Zhou, L.6    Mu, Y.L.7    Tang, W.8    Wang, Y.S.9
  • 8
    • 79953038616 scopus 로고    scopus 로고
    • Differential expression of the a2,3-sialic acid residues in breast cancer is associated with metastatic potential
    • Cui, H., Lin, Y., Yue, L., Zhao, X., and Liu, J. (2011) Differential expression of the a2,3-sialic acid residues in breast cancer is associated with metastatic potential. Oncol. Rep. 25, 1365-1371
    • (2011) Oncol. Rep. , Issue.25 , pp. 1365-1371
    • Cui, H.1    Lin, Y.2    Yue, L.3    Zhao, X.4    Liu, J.5
  • 9
    • 10644291062 scopus 로고    scopus 로고
    • Glycosylation of urinary prostate-specific antigen in benign hyperplasia and cancer: Assessment by lectin-binding patterns
    • Janković, M.M. and Kosanović, M.M. (2005) Glycosylation of urinary prostate-specific antigen in benign hyperplasia and cancer: Assessment by lectin-binding patterns. Clin. Biochem. 38, 58-65
    • (2005) Clin. Biochem. , vol.38 , pp. 58-65
    • Janković, M.M.1    Kosanović, M.M.2
  • 10
    • 61849174789 scopus 로고    scopus 로고
    • Glycoproteomics for prostate cancer detection: Changes in serum PSA glycosylation patterns
    • Meany, D.L., Zhang, Z., Sokoll, L.J., Zhang, H., and Chan, D.W. (2009) Glycoproteomics for prostate cancer detection: Changes in serum PSA glycosylation patterns. J. Proteome Res. 8, 613-619
    • (2009) J. Proteome Res. , vol.8 , pp. 613-619
    • Meany, D.L.1    Zhang, Z.2    Sokoll, L.J.3    Zhang, H.4    Chan, D.W.5
  • 11
    • 4444231395 scopus 로고    scopus 로고
    • Carbohydrate structure and differential binding of prostate specific antigen to Maackia amurensis lectin between prostate cancer and benign prostate hypertrophy
    • Ohyama, C., Hosono, M., Nitta, K., Oh-eda, M., Yoshikawa, K., Habuchi, T., Arai, Y., and Fukuda, M. (2004) Carbohydrate structure and differential binding of prostate specific antigen to Maackia amurensis lectin between prostate cancer and benign prostate hypertrophy. Glycobiology 14, 671-679
    • (2004) Glycobiology , vol.14 , pp. 671-679
    • Ohyama, C.1    Hosono, M.2    Nitta, K.3    Oh-eda, M.4    Yoshikawa, K.5    Habuchi, T.6    Arai, Y.7    Fukuda, M.8
  • 12
    • 0026020575 scopus 로고
    • Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis
    • Knibbs, R.N., Goldstein, I.J., Ratcliffe, R.M., and Shibuya, N. (1991) Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. J. Biol. Chem. 266, 83-88
    • (1991) J. Biol. Chem. , vol.266 , pp. 83-88
    • Knibbs, R.N.1    Goldstein, I.J.2    Ratcliffe, R.M.3    Shibuya, N.4
  • 13
    • 0028299382 scopus 로고
    • Strong affinity of Maackia amurensis hemagglutinin (MAH) for sialic acid-containing Ser/Thr-linked carbohydrate chains of N-terminal octapeptides from human glycophorin A
    • Konami, Y., Yamamoto, K., Osawa, T., and Irimura, T. (1994) Strong affinity of Maackia amurensis hemagglutinin (MAH) for sialic acid-containing Ser/Thr-linked carbohydrate chains of N-terminal octapeptides from human glycophorin A. FEBS Lett. 342, 334-338
    • (1994) FEBS Lett. , vol.342 , pp. 334-338
    • Konami, Y.1    Yamamoto, K.2    Osawa, T.3    Irimura, T.4
  • 14
    • 0031002992 scopus 로고    scopus 로고
    • Purification and carbohydrate-binding specificity of Agrocybe cylindracea lectin
    • Yagi, F., Miyamoto, M., Abe, T., Minami, Y., Tadera, K., and Goldstein, I.J. (1997) Purification and carbohydrate-binding specificity of Agrocybe cylindracea lectin. Glycoconj. J. 14, 281-288
    • (1997) Glycoconj. J. , vol.14 , pp. 281-288
    • Yagi, F.1    Miyamoto, M.2    Abe, T.3    Minami, Y.4    Tadera, K.5    Goldstein, I.J.6
  • 15
    • 23444442426 scopus 로고    scopus 로고
    • Structural basis of a fungal galectin from Agrocybe cylindracea for recognizing sialoconjugate
    • Ban, M., Yoon, H.J., Demirkan, E., Utsumi, S., Mikami, B., and Yagi, F. (2005) Structural basis of a fungal galectin from Agrocybe cylindracea for recognizing sialoconjugate. J. Mol. Biol. 351, 695-706
    • (2005) J. Mol. Biol. , vol.351 , pp. 695-706
    • Ban, M.1    Yoon, H.J.2    Demirkan, E.3    Utsumi, S.4    Mikami, B.5    Yagi, F.6
  • 16
    • 0022467156 scopus 로고
    • Frontal affinity chromatography: Theory, for its application to studies on specific interaction of biomolecules
    • Kasai, K., Oda, Y., Nishikawa, M., and Ishii, S. (1986) Frontal affinity chromatography: Theory, for its application to studies on specific interaction of biomolecules. J. Chromatogr. 376, 33-47
    • (1986) J. Chromatogr. , vol.376 , pp. 33-47
    • Kasai, K.1    Oda, Y.2    Nishikawa, M.3    Ishii, S.4
  • 17
    • 0035497421 scopus 로고    scopus 로고
    • Agrocybe cylindracea lectin is a member of the galectin family
    • Yagi, F., Hiroyama, H., and Kodama, S. (2001) Agrocybe cylindracea lectin is a member of the galectin family. Glycoconj. J. 18, 745-749
    • (2001) Glycoconj. J. , vol.18 , pp. 745-749
    • Yagi, F.1    Hiroyama, H.2    Kodama, S.3
  • 18
    • 20444460776 scopus 로고    scopus 로고
    • Comparative analysis of carbohydrate-binding properties of two tandem repeat-type Jacalin-related lectins, Castanea crenata agglutinin and Cycas revoluta leaf lectin
    • Nakamura, S., Yagi, F., Otani, K., Ito, Y., and Hirabayashi, J. (2005) Comparative analysis of carbohydrate-binding properties of two tandem repeat-type Jacalin-related lectins, Castanea crenata agglutinin and Cycas revoluta leaf lectin. FEBS J. 272, 2784-2799
    • (2005) FEBS J. , vol.272 , pp. 2784-2799
    • Nakamura, S.1    Yagi, F.2    Otani, K.3    Ito, Y.4    Hirabayashi, J.5
  • 19
    • 38449103336 scopus 로고    scopus 로고
    • Frontal affinity chromatography: Sugar-protein interactions
    • Tateno, H., Nakamura-Tsuruta, S., and Hirabayashi, J. (2007) Frontal affinity chromatography: Sugar-protein interactions. Nat. Protoc. 2, 2529-2799
    • (2007) Nat. Protoc. , vol.2 , pp. 2529-2799
    • Tateno, H.1    Nakamura-Tsuruta, S.2    Hirabayashi, J.3
  • 20
    • 0001380051 scopus 로고
    • Isolation and properties of N-acetyllactosamine-specific lectins from nine erythrina species
    • Lis, H., Joubert, F.J., and Sharon, N. (1985) Isolation and properties of N-acetyllactosamine-specific lectins from nine erythrina species. Phytochemistry 24, 2803-2809
    • (1985) Phytochemistry , vol.24 , pp. 2803-2809
    • Lis, H.1    Joubert, F.J.2    Sharon, N.3
  • 22
    • 33750309519 scopus 로고    scopus 로고
    • Comparative analysis by frontal affinity chromatography of oligosaccharide specificity of GlcNAc-binding lectins Griffonia simplicifolia lectin-II (GSL-II) and Boletopsis leucomelas lectin (BLL)
    • Nakamura-Tsuruta, S., Kominami, J., Kamei, M., Koyama, Y., Suzuki, T., Isemura, M., and Hirabayashi, J. (2006) Comparative analysis by frontal affinity chromatography of oligosaccharide specificity of GlcNAc-binding lectins, Griffonia simplicifolia lectin-II (GSL-II) and Boletopsis leucomelas lectin (BLL). J. Biochem. 140, 285-291
    • (2006) J. Biochem. , vol.140 , pp. 285-291
    • Nakamura-Tsuruta, S.1    Kominami, J.2    Kamei, M.3    Koyama, Y.4    Suzuki, T.5    Isemura, M.6    Hirabayashi, J.7
  • 23
    • 77956640648 scopus 로고    scopus 로고
    • Frontal affinity chromatography analysis of constructs of DC-DIGNR and LSECtin extend evidence for affinity to agalactosylated N-glycans
    • Yabe, R., Tateno, H., and Hirabayashi, J. (2010) Frontal affinity chromatography analysis of constructs of DC-DIGNR and LSECtin extend evidence for affinity to agalactosylated N-glycans. FEBS J. 277, 4010-4026
    • (2010) FEBS J. , vol.277 , pp. 4010-4026
    • Yabe, R.1    Tateno, H.2    Hirabayashi, J.3
  • 27
    • 5144232009 scopus 로고    scopus 로고
    • Growth-regulatory human galectin-1: Crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding
    • López-Lucendo, M.F., Solís, D., André, S., Hirabayashi, J., Kasai, K., Kaltner, H., Gabius, H.J., and Romero, A. (2004) Growth-regulatory human galectin-1: Crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J. Mol. Biol. 343, 957-970
    • (2004) J. Mol. Biol. , vol.343 , pp. 957-970
    • López-Lucendo, M.F.1    Solís, D.2    André, S.3    Hirabayashi, J.4    Kasai, K.5    Kaltner, H.6    Gabius, H.J.7    Romero, A.8
  • 29
    • 0033607322 scopus 로고    scopus 로고
    • The 2.15 A° crystal structure of CG-16, the developmentally regulated homodimeric chicken galectin
    • Varela, P.F., Solís, D., Díaz-Mauriño, T., Kaltner, H., Gabius, H.J., and Romero, A. (1999) The 2.15 A° crystal structure of CG-16, the developmentally regulated homodimeric chicken galectin. J. Mol. Biol. 294, 537-549
    • (1999) J. Mol. Biol. , vol.294 , pp. 537-549
    • Varela, P.F.1    Solís, D.2    Díaz-Maurino, T.3    Kaltner, H.4    Gabius, H.J.5    Romero, A.6
  • 30
    • 0033570024 scopus 로고    scopus 로고
    • High-resolution structure of the conger eel galectin, congerin I, in lactose liganded and ligand-free forms: Emergence of a new structure class by accelerated evolution
    • Shirai, T., Mitsuyama, C., Niwa, Y., Matsui, Y., Hotta, H., Yamane, T., Kamiya, H., Ishii, C., Ogawa, T., and Muramoto, K. (1999) High-resolution structure of the conger eel galectin, congerin I, in lactose liganded and ligand-free forms: Emergence of a new structure class by accelerated evolution. Struct. Fold. Des. 7, 1223-1233
    • (1999) Struct. Fold. Des. , vol.7 , pp. 1223-1233
    • Shirai, T.1    Mitsuyama, C.2    Niwa, Y.3    Matsui, Y.4    Hotta, H.5    Yamane, T.6    Kamiya, H.7    Ishii, C.8    Ogawa, T.9    Muramoto, K.10
  • 31
    • 0022854422 scopus 로고
    • Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian b-galactosides
    • Leffler, H. and Barondes, SH. (1986) Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian b-galactosides. J. Biol. Chem. 261, 10119-10126
    • (1986) J. Biol. Chem. , vol.261 , pp. 10119-10126
    • Leffler, H.1    Barondes, S.H.2
  • 32
    • 0030447353 scopus 로고    scopus 로고
    • The primary structure and carbohydrate specificity of a b-galactosyl-binding lectin from toad (Bufo arenarum Hensel) ovary reveal closer similarities to the mammalian galectin-1 than to the galectin from the clawed frog Xenopus laevis
    • Ahmed, H., Pohl, J., Fink, NE., Strobel, F., and Vasta, GR. (1996) The primary structure and carbohydrate specificity of a b-galactosyl-binding lectin from toad (Bufo arenarum Hensel) ovary reveal closer similarities to the mammalian galectin-1 than to the galectin from the clawed frog Xenopus laevis. J. Biol. Chem. 271, 33083-33094
    • (1996) J. Biol. Chem. , vol.271 , pp. 33083-33094
    • Ahmed, H.1    Pohl, J.2    Fink, N.E.3    Strobel, F.4    Vasta, G.R.5
  • 34
    • 0035956948 scopus 로고    scopus 로고
    • Mutated plant lectin library useful to identify different cells
    • Yim, M., Ono, T., and Irimura, T. (2001) Mutated plant lectin library useful to identify different cells. Proc. Natl. Acad. Sci. USA. 98, 2222-2225
    • (2001) Proc. Natl. Acad. Sci. USA. , vol.98 , pp. 2222-2225
    • Yim, M.1    Ono, T.2    Irimura, T.3
  • 35
    • 50449103704 scopus 로고    scopus 로고
    • Use of a library of mutated Maackia amurensis hemagglutinin for profiling the cell lineage and differentiation
    • Maenuma, K., Yim, M., Komatsu, K., Hoshino, M., Takahashi, Y., Bovin, N., and Irimura, T. (2008) Use of a library of mutated Maackia amurensis hemagglutinin for profiling the cell lineage and differentiation. Proteomics 8, 3274-3283
    • (2008) Proteomics , vol.8 , pp. 3274-3283
    • Maenuma, K.1    Yim, M.2    Komatsu, K.3    Hoshino, M.4    Takahashi, Y.5    Bovin, N.6    Irimura, T.7
  • 36
    • 67650351496 scopus 로고    scopus 로고
    • A library of mutated Maackia amurensis hemagglutinin distinguishes putative glycoforms of immunoglobulin A1 from IgA nephropathy patients
    • Maenuma, K., Yim, M., Komatsu, K., Hoshino, M., Tachiki-Fujioka, A., Takahashi, K., Hiki, Y., Bovin, N., and Irimura, T. (2009) A library of mutated Maackia amurensis hemagglutinin distinguishes putative glycoforms of immunoglobulin A1 from IgA nephropathy patients. J. Proteome Res. 8, 3617-3624
    • (2009) J. Proteome Res. , vol.8 , pp. 3617-3624
    • Maenuma, K.1    Yim, M.2    Komatsu, K.3    Hoshino, M.4    Tachiki-Fujioka, A.5    Takahashi, K.6    Hiki, Y.7    Bovin, N.8    Irimura, T.9
  • 37
    • 34248679037 scopus 로고    scopus 로고
    • Tailoring a novel sialic acid-binding lectin from a ricin-B chain-like galactose-binding protein by natural evolution-mimicry
    • Yabe, R., Suzuki, R., Kuno, A., Fujimoto, Z., Jigami, Y., and Hirabayashi, J. (2007) Tailoring a novel sialic acid-binding lectin from a ricin-B chain-like galactose-binding protein by natural evolution-mimicry. J. Biochem. 141, 389-399
    • (2007) J. Biochem. , vol.141 , pp. 389-399
    • Yabe, R.1    Suzuki, R.2    Kuno, A.3    Fujimoto, Z.4    Jigami, Y.5    Hirabayashi, J.6


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