Leaves of the Lamiaceae species Glechoma hederacea (ground ivy) contain a lectin that is structurally and evolutionary related to the legume lectins

Plant Journal

Volumn 33, Issue 2, 2003, Pages 293-304

  Wang, Weifang ^a,f   Peumans, Willy J ^a   Rougé, Pierre ^b   Rossi, Claire ^b   Proost, Paul ^c   Chen, Jianping ^d   Van Damme, Els J M ^a,e  

^a UNIVERSITY OF LEUVEN   (Belgium)

^b CNRS   (France)

^c REGA INSTITUTE FOR MEDICAL RESEARCH   (Belgium)

^d INSTITUTE OF PLANT PROTECTION AND MICROBIOLOGY   (China)

^e GHENT UNIVERSITY   (Belgium)

^f ZHEJIANG UNIVERSITY   (China)

Author keywords

cDNA cloning; Glechoma hederacea; Lamiaceae; Legume lectin; Molecular evolution; N acetylgalactosamine binding

Indexed keywords

AMINES; CLONING; PHYSIOLOGY; PROTEINS;

BIOCHEMICAL ANALYSIS;

PLANTS (BOTANY);

AMINO ACID SEQUENCE; ANIMALS; CARBOHYDRATE METABOLISM; EVOLUTION, MOLECULAR; FABACEAE; HEMAGGLUTINATION; HUMANS; LAMIACEAE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLANT LEAVES; PLANT LECTINS; PROTEIN BINDING; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EMBRYOPHYTA; GLECHOMA HEDERACEA; HEDERA; LAMIACEAE; MAGNOLIOPHYTA;

EID: 0037263581     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.2003.01623.x     Document Type: Article

References (43)

1. Alperin, D.M., Latter, H., Lis, H. and Sharon, N. (1992) Isolation, by affinity chromatography and gel filtration in 8 M urea, of an active subunit from the anti-(blood group A+N)-specific lectin of Molucella laevis. Biochem. J. 285, 1-4.
2. Barre, A., Hervé, C., Lescure, B. and Rougé, P. (2002) Lectin receptor kinases in plants. Crit. Rev. Plant Sci. 21, 379-399.
3. Bourne, Y., Abergel, C., Cambillau, C., Frey, M., Rougé, P. and Fontecilla-Camps, J.C. (1990) X-ray crystal structure determination and refinement at 1.9 Å resolution of isolectin I from the seeds of Lathyrus ochrus. J. Mol. Biol. 214, 571-584.
4. Brewin, N.J. and Kardailsky, I.V. (1997) Legume lectins and nodulation by Rhizobium. Trends Plant Sci. 2, 92-98.
5. Diaz, C., Melchers, L.S., Hooykaas, P.J.J., Lugtenberg, B.J.J. and Kijne, J.W. (1989) Root lectin as a determinant of host-plant specificity in the Rhizobium-legume symbiosis. Nature, 338, 579-581.
6. Dubois, M., Gilles, K.A., Hamilton, J.K., Rebers, P.A. and Smith, F. (1956) Colorimetric method for determination of sugar and related substances. Anal. Chem. 28, 350-356.
7. Elgavish, S. and Shaanan, B. (1998) Structures of the Erythrina corallodendron lectin and of its complexes with mono- and disaccharides. J. Mol. Biol. 277, 917-932.
8. Esnouf, R.M. (1997) An extensively modified version of Molscript that includes greatly enhanced coloring capabilities. J. Mol. Graphics, 15, 132-134.
9. Fabre, C., Causse, H., Mourey, L., Koninkx, J., Riviėre, M., Hendriks, H., Puzo, G., Samama, J.P. and Rougė, 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.
10. 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.
11. Gilson, M.K. and Honing, B.H. (1987) Calculation of electrostatic potential in an enzyme active site. Nature, 330, 84-86.
12. Gouet, P., Courcelle, E., Stuart, D.I. and Metoz, F. (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics, 15, 305-308.
13. Hamelryck, T.W., Poortmans, F., Goossens, A., Angenon, G., Van Montagu, M., Wyns, L. and Loris, R. (1996) Crystal structure of arcelin-5, a lectin-like defense protein from Phaseolus vulgaris. J. Biol. Chem. 271, 32796-32802.
14. von Heijne, G. (1986) A method for predicting signal sequence cleavage sites. Nucl. Acids Res. 11, 4683-4690.
15. Hervé, C., Dabos, P., Gallaud, J.P., Rougé, P. and Lescure, B. (1996) Characterization of an Arabidopsis thaliana gene that defines a new class of plant receptor kinases with an extracellular lectin-like domain. J. Mol. Biol. 258, 778-788.
16. Hirsch, A.M. (1999) Role of lectins (and rhizobial exopolysaccharides) in legume nodulation. Curr. Opin. Plant Biol. 2, 320-326.
17. Hirsch, A.M., Lum, M.R. and Downie, J.A. (2001) What makes the Rhizobia-legume symbiosis so special? Plant Physiol. 127, 1484-1492.
18. Kitagaki-Ogawa, H., Matsumoto, I., Seno, N., Takahashi, N., Endo, S. and Arata, Y. (1986) Characterization of the carbohydrate moiety of Clerodendrum trichotomum lectins. Its structure and reactivity toward plant lectins. Eur. J. Biochem. 161, 779-785.
19. Kraulis, P.J. (1991) Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
20. 4. Nature, 227, 680-685.
21. 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. Cryst. 26, 283-291.
22. 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.
23. Lis, H. and Sharon, N. (1994) Molucella laevis lectin - an unusual protein with a unique specificity. Trends Glycosci. Glycotechnol. 6, 65-74.
24. Maniatis, T., Fritsch, E.F. and Sambrook, J. (1982) Molecular Cloning: a Laboratory Manual Cold Spring Harbor, New York: Cold Spring Harbor Laboratory.
25. Mas, M.T., Smith, K.C., Yarmush, D.L., Aísaka, 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.
26. Medeiros, A., Bianchi, S., Calvete, J.J., Balter, H., Bay, S., Robles, A., Cantacuzėne, D., Nimtz, M., Alzari, P.M. and Osinaga, E. (2000) Biochemical and functional characterization of the Tn-specific lectin from Salvia sclarea seeds. Eur. J. Biochem. 267, 1434-1440.
27. Merritt, E.A. and Bacon, D.J. (1997) Raster3D photorealistic molecular graphics. Meth. Enzymol. 277, 505-524.
28. Mierendorf, R.C. and Pfeffer, D. (1987) Direct sequencing of denatured plasmid DNA. Meth. Enzymol. 152, 556-562.
29. 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.
30. Nicholls, A., Sharp, K.A. and Honig, B. (1991) Protein folding and association: insights from the interracial and thermodynamic properties of hydrocarbons. Proteins Struc. Func. Genet, 11, 281-296.
31. 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.
32. Reveal, J.L. (1998) Cronquist system of angiosperm classification. http://www.inform.umd.edu./PBIO/pb250.
33. Roberts, N.J., Brigham, J., Wu, B., Murphy, J.B., Volpin, H., Phillips, D.A. and Etzler, M.E. (1999) A Nod factor-binding lectin is a member of a distinct class of apyrases that may be unique to the legumes. Mol. Gen. Genet. 262, 261-267.
34. Sanger, F., Nicklen, S. and Coulson, A.R. (1977) DNA sequencing with chain terminating inhibitors. Proc. Natl Acad. Sci. USA, 74, 5463-5467.
35. Shaanan, B., Lis, H. and Sharon, N. (1991) Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose. Science, 254, 862-866.
36. 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.
37. Sharon, N. and Lis, H. (1990) Legume lectins - a large family of homologous proteins. FASEB J. 4, 3198-3208.
38. Sreerama, N., Venyaminov, S.Y. and Woody, R.W. (1999) Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8, 370-380.
39. 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. Nucl Acids Res. 15, 4876-4882.
40. 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.
41. 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.
42. 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.
43. Zhang, W., Peumans, W.J., Barre, A., Houles-Astoul, C., Rovira, P., Rougé, P., Proost, P., Truffa-Bachi, P., Jalali, A.A.H. 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.