The size, shape and specificity of the sugar-binding site of the jacalin-related lectins is profoundly affected by the proteolytic cleavage of the subunits

Biochemical Journal

Volumn 367, Issue 3, 2002, Pages 817-824

  Houlès Astoul, Corinne ^a   Peumans, Willy J ^a   Van Damme, Els J M ^a   Barre, Annick ^a   Bourne, Yves ^a   Rougé, Píerre ^a  

^a CNRS   (France)

Author keywords

Carbohydrate binding proteins; Galactose; Mannose; Plant proteins; Processing

Indexed keywords

BIOSYNTHESIS; CARBOHYDRATES; PLANTS (BOTANY); PROTEINS; SUGAR (SUCROSE); SURFACE PLASMON RESONANCE;

PROTEOLYTIC CLEAVAGE;

BIOCHEMISTRY;

AGGLUTININ; CARBOHYDRATE BINDING PROTEIN; GALACTOSE; JACALIN; JACALIN RELATED LECTIN; LECTIN; MANNOSE; N ACETYLGALACTOSAMINE; PROTEIN SUBUNIT; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; ASTERACEAE; BINDING SITE; BIOSYNTHESIS; BRASSICA; CONTROLLED STUDY; CONVOLVULACEAE; MORACEAE; MUSACEAE; NONHUMAN; OLIGOMERIZATION; PLANT DISEASE; POACEAE; PREDATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN LOCALIZATION; PROTEIN PROCESSING; PROTEIN STRUCTURE; SURFACE PLASMON RESONANCE;

BINDING SITES; CARBOHYDRATE METABOLISM; HYDROLYSIS; MANNOSE; PLANT LECTINS; PROTEIN CONFORMATION; PROTEIN FOLDING; SURFACE PLASMON RESONANCE;

ASTERACEAE; BRASSICA; BRASSICACEAE; CONVOLVULACEAE; EMBRYOPHYTA; MACLURA POMIFERA; MORACEAE; MUSACEAE; POACEAE;

EID: 0036846005     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020856     Document Type: Article

References (53)

1. Van Damme, E. J. M., Peumans, W. J., Barre, A. and Rougé, P. (1998) Plant lectins: A composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles. Crit. Rev. Plant Sci. 17, 575-692
2. Goldstein, I. J. and Poretz, R. D. (1986) Isolation, physicochemical characterization, and carbohydrate-binding specificity of lectins. In The Lectins, Properties, Functions, and Applications in Biology and Medicine (Liener, I. E., Sharon, N. and Goldstein, I. J., eds.), pp. 33-247, Academic Press, Orlando, FL
3. Transue, T. R., Smith, A. K., Mo, H., Goldstein, I. J. and Saper, M. A. (1997) Structure of benzyl T-antigen disaccharide bound to Amaranthus caudatus lectin. Nat. Struct. Biol. 10, 779-783
4. Rinderle, S. J., Goldstein, I. J., Marta, K. L. and Ratcliffe, R. M. (1989) Isolation anal characterization of amaranthin, a lectin present in the seeds of Amaranthus caudatus, that recognizes the T- (or cryptic T)-antigen. J. Biol. Chem. 264, 16123-16131
5. Barre, A., Van Damme, E. J. M., Peumans, W. J. and Rougé, P. (1996) Structure-function relationship of monocot mannose-binding lectins. Plant Physiol. 112, 1531-1540
6. Van Damme, E. J. M., Barre, A., Rougé, P., Van Leuven F. and Peumans, W. J. (1996) The NeuAc(α-2,6)-Gal/GalNAc binding lectin from elderberry (Sambucus nigra) bark is a type 2 ribosome inactivating protein with an unusual specificity arld structure. Eur. J. Biochem. 235, 128-137
7. Van Damme, E. J. M., Roy, S., Barre, A., Citores, L., Mostafapous, K., Rougé, P., Van Leuven, F., Girbes, T., Goldstein, I. J. and Peumans, W. J. (1997) Elderberry (Sambucus nigra) bark contains two structurally different Neu5Ac(α2,6)Gal/GalNAc-binding type 2 ribosome-inactivating proteins. Eur. J. Biochem. 245, 648-655
8. Rini, J. (1995) Lectin structure. Annu. Rev. Biophys. Biomol. Struct. 24, 551-577
9. Loris, R., Hamelryck, T., Bouckaert, J. and Wyns, L. (1998) Legume lectin structure. Biochim. Biophys. Acta 1383, 9-36
10. Young, N. M. and Oomen, R. P. (1992) Analysis of sequence variation among legume lectins. A ring of hypervariable residues forms the perimeter of the carbohydrate-binding site. J. Mol. Biol. 228, 924-934
11. Sharma, V. and Surolia, A. (1997) Analyses of carbohydrate recognition by legume lectins: Size of the combining site loops and their primary specificity. J. Mol. Biol. 267, 433-445
12. Sankaranarayanan, R., Sekar, K., Banerjee, R., Sharma, V., Surolia, A. and Vijayan, M. (1996) A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a β-prism fold. Nat. Struct. Biol. 3, 596-603
13. Lee, X., Thompson, A., Zhang, Z., Ton-That, H., Biesterfeldt, J., Ogata, C., Xu, L., Johnston, A. Z. and Young, N. M. (1998) Structure of the complex of Maclura pomifera agglutinin and the T-antigen disaccharide, Galβ1,3GalNAc. J. Biol. Chem. 273, 6312-6318
14. Moreira, R. A. and Ainouz, I. L. (1981) Lectins from seeds of jack fruit (Artocarpus integrifolia L.): isolation and purification of two isolectins from the albumin fraction. Biol. Plant (Praha) 23, 186-192
15. Bausch, J. N. and Poretz, R. D. (1977) Purification and properties of the hemagglutinin from Maclura pomifera seeds. Biochemistry 16, 5790-5794
16. Van Damme, E. J. M., Barre, A., Verhaert, P., Rougé, P. and Peumans, W. J. (1996) Molecular cloning of the mitogenic mannose/maltose-specific rhizome lectin from Calystegia sepium. FEBS Lett. 397, 352-356
17. Peumans, W. J., Winter, H. C., Bemer, V., Van Leuven, F., Goldstein, I. J., Truffa-Bachi, P. and Van Damme, E. J. M. (1997) Isolation of a novel plant lectin with an unusual specificity from Calystegia sepium. Glycoconj. J. 14, 259-265
18. Van Damme, E. J. M., Barre, A., Mazard, A.-M., Verhaert, P., Horman, A., Debray, H., Rougé, P. and Peumans, W. J. (1999) Characterization and molecular cloning of the lectin from Helianthus tuberosus. Eur. J. Biochem. 259, 135-142
19. Claes, B., Dekeyser, R., Villarroel, R., Van den Bulcke, M., Bauw, G., Van Montagu, M. and Caplan, A. (1990) Characterization of a rice gene showing organ-specific expression in response to salt stress and drought. Plant Cell 2, 19-27
20. Zhang, W., Peumans, W. J., Barre, A., Houles Astoul, C., Rovira, P., Rougé, P., Proost, P., Truffa-Bachi, P., Jalali, H. A. and Van Damme, E. J. M. (2000) Isolation and characterization of a jacalin-related mannose-binding lectin from salt-stressed rice (Oryza sativa) plants. Planta 210, 970-978
21. Clendennen, S. K. and May, G. D. (1997) Differential gene expression in ripening banana fruit. Plant Physiol. 115, 463-469
22. Peumans, W. J., Zhang, W., Barre, A., Houles Astoul, C., Balint-Kurti, P. J., Rovira, P., Rougé, P., May, G. D., Van Leuven, F., Truffa-Bachi, P. and Van Damme, E. J. M. (2000) Fruit-specific lectins from banana and plantain. Planta 211, 546-554
23. Nomura, K., Nakamura, S., Fujitake, M. and Nakanishi, T. (2000) Complete amino acid sequence of Japanese chestnut agglutinin. Biochem. Biophys. Res. Commun. 276, 23-28
24. Mann, K., Farias, C. M. S. A., Gallego Del Sol, F., Santos, C. F., Grangeiro, T. B., Nagano, C. S., Cavada, B. S. and Calvete, J. J. (2001) The amino-acid sequence of the glucose/mannose-specific lectin isolated from Parkia platycephala seeds reveals three tandemly arranged jacalin-related domains. Eur. J. Biochem. 268, 4414-4422
25. Geshi, N. and Brandt, A. (1998) Two jasmonate-inducible myrosinase-binding proteins from Brassica napus L. seedlings with homology to jacalin. Planta 204, 295-304
26. Yang, H. and Czapla, T. H. (1993) Isolation and characterization of cDNA clones encoding jacalin isolectins. J. Biol. Chem. 268, 5905-5910
27. Peumans, W. J., Hause, B. and Van Damme, E. J. M. (2000) The galactose-binding and mannose-binding jacalin-related lectins are located in different sub-cellular compartments. FEBS Lett. 477, 186-192
28. Sastry, M. V. K., Banerjee, P., Patanjali, S. R., Swamy, M. J., Swarnalatha, G. V. and Surolia, A. (1986) Analysis of the saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (β-D-Gal(1,3)D-GalNAc). J. Biol. Chem. 261, 11726-11733
29. Sarkar, M., Wu, A. M. and Kabat, E. A. (1981) Immunochemical studies on the carbohydrate specificity of Maclura pomifera lectin. Arch. Biochem. Biophys. 209, 204-218
30. Bourne, Y., Zamboni, V., Barre, A., Peumans, W. J., Van Damme, E. J. M. and Rougé, P. (1999) Helianthus tuberosus lectin, the crystal structure reveals a widespread scaffold for mannose-binding lectins. Structure Fold. Des. 7, 1473-1482
31. Bourne, Y., Houlès Astoul, C., Zamboni, V., Peumans, W. J., Menu-Bouaouiche, L., Van Damme, E. J. M., Barre, A. and Rougé, P. (2002) Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose. Biochem. J. 364, 173-179
32. Montreuil, J. (1984) Spatial conformation of glycans and glycoproteins. Biol. Cell 51, 115-132
33. Naismith, J. H. and Field, R. A. (1996) Structural basis of trimannoside recognition by concanavalin A. J. Biol. Chem. 271, 972-976
34. Edge, A. S. B. and Spiro, R. G. (1987) Presence of an O-glycosidically linked hexasaccharide in fetuin. J. Biol. Chem. 262, 16135-16141
35. Cummings, D. A., Hellerqvist, C. G., Harris-Brandts, M., Michnick, S. W., Carver, J. P. and Bendiak, B. (1989) Structures of asparagine-linked oligosaccharides of the glycoprotein fetuin having sialic acid linked to N-acetylglucosamine. Biochemistry 28, 6500-6512
36. 1H-NMR spectroscopy. J. Biol. Chem. 256, 7708-7711
37. Dessen, A., Gupta, D., Sabesan, S., Brewer, C. F. and Sacchettini, J. C. (1995) X-ray crystal structure of the soybean agglutinin cross-linked with a biantennary analog of the blood group I carbohydrate antigen. Biochemistry 34, 4933-4942
38. Mourey, L., Pédelacq, J. D., Birck, C., Fabre, C., Rougé, P. and Samama, J. P. (1998) Crystal structure of arcelin-1 from Phaseolus vulgaris at 1.9 Å resolution. J. Biol. Chem. 273, 12914-12922
39. Bourne, Y., Mazurier, J., Legrand, D., Rougé, P., Montreuil, J., Spik, G. and Cambillau, C. (1994) Interaction of a legume lectin with the human lactotransferrin N2 fragment or with the isolated biantennary glycopeptide: Role of the fucose moiety. Structure 2, 209-219
40. Hester, G., Kaku, H., Goldstein, I. J. and Wright, C. S. (1995) Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family. Nat. Struct. Biol. 2, 472-479
41. Pratap, J. V., Jeyaprakash, A. A., Rani, P. G., Sekar, K., Surolia, A. and Vijayan, M. (2002) Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-α-o-mannose: Implications to the generation of carbohydrate specificity. J. Mol. Biol. 317, 237-247
42. Rosa, J. C., De Oliveira, P. S. L., Garratt, R., Beltramini, L., Resing, K., Roque-Barreira, M.-C. and Greene, L. J. (1999) KM +, a mannose-binding lectin from Artocarpus integrifolia: Amino acid sequence, predicted tertiary structure, carbohydrate recognition, and analysis of the β-prism fold. Protein Sci. 8, 13-24
43. Allen, A. K. and Neuberger, A. (1975) A simple method for the preparation of an affinity adsorbent for soybean agglutinin using galactosamine and CH-Sepharose. FEBS Lett. 50, 362-364
44. Fabre, C., Causse, H., Mourey, L., Koninkx, J., Rivière, M., Hendriks, H., Puzo, G., Samama, J. P. and Rougé, P. (1998) Characterization and sugar-binding properties of arcelin-1, an insecticidal lectin-like protein isolated from kidney bean (Phaseolus vulgaris L. cv RAZ-2) seeds. Biochem. J. 329, 551-560
45. Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F. and Higgins, D. G. (1997) The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tool. Nucleic Acids Res. 15, 4876-4882
46. Gaboriaud, C., Bissery, V., Benchetrit, T. and Mornon, J. P. (1987) Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences. FEBS Lett. 224, 149-155
47. Lemesle-Varloot, L., Henrissat, B., Gaboriaud, C., Bissery, V., Morgat, A. and Mornon, J. P. (1990) Hydrophobic cluster analysis procedure to derive structural and functional information from 2-D-representation of protein sequences. Biochimie 72, 555-574
48. Ponder, J. W. and Richards, F. M. (1987) Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 193, 775-791
49. Mas, M. T., Smith, K. C., Yarmush, D. L., Aisaka, K. and Fine, R. M. (1992) Modeling the anti-CEA antibody combining site by homology and conformational search. Proteins Struct. Funct. Genet. 14, 483-498
50. Laskowski, R. A., MacArthur, M. W., Moss, D. S. and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemistry of protein structures. J. Appl. Crystallogr. 26, 283-291
51. Kraulis, P. J. (1991) Molscript: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950
52. Esnouf, R. M. (1997) An extensively modified version of Molscript that includes greatly enhanced coloring capabilities. J. Mol. Graphics 15, 132-134
53. Merritt, E. A. and Bacon, D. J. (1997) Raster3D photorealistic molecular graphics. Methods Enzymol. 277, 505-524