Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 72, 2008 - Issue 10
Journal homepage
1,083
Views
17
CrossRef citations to date
0
Altmetric
Original Articles

Molecular Structure and Properties of Lectin from Tomato Fruit

Suguru OGURIDepartment of Bioproduction, Faculty of Bioindustry, Tokyo University of Agriculture
,
Koh AMANOResearch Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST)
,
Hideo NAKASHITAPlant Acquired Immunity Research Unit, Discovery Research Institute, RIKEN
,
Yoshiho NAGATADepartment of Bioresources Chemistry, Faculty of Horticulture, Chiba University
&
Yoshie S. MOMONOKIDepartment of Bioproduction, Faculty of Bioindustry, Tokyo University of Agriculture
Pages 2640-2650 | Received 07 May 2008, Accepted 23 Jun 2008, Published online: 22 May 2014

  • 1) Nachbar, M. S., Oppenheim, J. D., and Thomas, J. O., Lectins in the U.S. Diet. Isolation and characterization of a lectin from the tomato (Lycopersicon esculentum). J. Biol. Chem., 255, 2056–2061 (1980).
  • 2) Kilpatrick, D. C., Purification and some properties of a lectin from the fruit juice of the tomato (Lycopersicon esculentum). Biochem. J., 185, 269–272 (1980).
  • 3) Merkle, R. K., and Cummings, R. D., Tomato lectin is located predominantly in the locular fluid of ripe tomatoes. Plant Cell, 48, 71–78 (1987).
  • 4) Saito, K., Yagi, H., Baba, K., Goldstein, I. J., and Misaki, A., Purification, properties and carbohydrate-binding specificity of cherry tomato (Lycopersicon esculentum var. Cherry) lectin. Oyo Toshitsu Kagaku (J. Appl. Glycosci.), 43, 331–345 (1996).
  • 5) Naito, Y., Minamihara, T., Ando, A., Marutani, T., Oguri, S., and Nagata, Y., Domain construction of cherry-tomato lectin: relation to newly found 42-kDa protein. Biosci. Biotechnol. Biochem., 65, 86–93 (2001).
  • 6) Saitoh, O., Wang, W. C., Lotan, R., and Fukuda, M., Differential glycosylation and cell surface expression of lysosomal membrane glycoproteins in sublines of a human colon cancer exhibiting distinct metastatic potentials. J. Biol. Chem., 267, 5700–5711 (1992).
  • 7) Bankston, P. W., Porter, G. A., Milici, A. J., and Palade, G. E., Differential and specific labeling of epithelial and vascular endothelial cells of the rat lung by Lycopersicon esculentum and Griffonia simplicifolia I lectins. Eur. J. Cell Biol., 54, 187–195 (1991).
  • 8) Woodley, J. F., Lectins for gastrointestinal targeting—15 years on. J. Drug Target., 7, 325–333 (2000).
  • 9) Raikhel, N. V., and Lee, H. I., Structure and function of chitin-binding proteins. Annu. Rev. Plant Physiol. Plant Mol. Biol., 44, 591–615 (1993).
  • 10) Czapla, T., and Lang, B., Effect of plant lectins on the larval development of european corn borer (Lepidoptera: Pyraidae) and southern corn rootworm (Coleoptera: Chrysomelidae). J. Econ. Entomol., 83, 2480–2485 (1990).
  • 11) Schlumbaum, A., Mauch, F., Vögeli, U., and Boller, T., Plant chitinases are potent inhibitors of fungal growth. Nature, 324, 365–367 (1986).
  • 12) Oguri, S., Analysis of sugar chain-binding specificity of tomato lectin using lectin blot: recognition of high mannose-type N-glycans produced by plants and yeast. Glycoconj. J., 22, 453–461 (2005).
  • 13) Kieliszewski, M. J., Showalter, A. M., and Leykam, J. F., Potato lectin: a modular protein sharing sequence similarities with the extensin family, the hevein lectin family, and snake venom disintegrins (platelet aggregation inhibitors). Plant J., 5, 849–861 (1994).
  • 14) Allen, A. K., Bolwell, G. P., Brown, D. S., Sidebottom, C., and Slabas, A. R., Potato lectin: a three-domain glycoprotein with novel hydroxyproline-containing sequences and sequence similarities to wheat-germ agglutinin. Int. J. Biochem. Cell Biol., 28, 1285–1291 (1996).
  • 15) Ashford, D., Desai, N. N., Allen, A. K., Neuberger, A., O’Neill, M. A., and Selvendran, R. R., Structural studies of the carbohydrate moieties of lectins from potato (Solanum tuberosum) tubers and thorn-apple (Datura stramonium) seeds. Biochem. J., 201, 199–208 (1982).
  • 16) Lerner, D. R., and Raikhel, N. V., The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase. J. Biol. Chem., 267, 11085–11091 (1992).
  • 17) Smith, J. J., and Raikhel, N. V., Nucleotide sequences of cDNA clones encoding wheat germ agglutinin isolectins A and D. Plant Mol. Biol., 13, 601–603 (1989).
  • 18) Kilpatrick, D. C., Graham, C., Urbaniak, S. J., Jeffree, C. E., and Allen, A. K., A comparison of tomato (Lycopersicon esculentum) lectin with its deglycosylated derivative. Biochem. J., 220, 843–847 (1984).
  • 19) Kieliszewski, M. J., and Orlando, R., Matrix assisted laser desorption/ionization time-of-flight mass spectrometry of tomato extensin monomers and potato lectin. Phytochemistry, 45, 9–14 (1997).
  • 20) Peumans, W. J., Rouge, P., and Van Damme, E. J., The tomato lectin consists of two homologous chitin-binding modules separated by an extensin-like linker. Biochem. J., 376, 717–724 (2003).
  • 21) Edge, A. S., Faltynek, C. R., Hof, L., Reichert, L. E., Jr., and Weber, P., Deglycosylation of glycoproteins by trifluoromethanesulfonic acid. Anal. Biochem., 118, 131–137 (1981).
  • 22) Bendtsen, J. D., Nielsen, H., von Heijne, G., and Brunak, S., Improved prediction of signal peptides: signalP 3.0. J. Mol. Biol., 340, 783–795 (2004).
  • 23) Showalter, A. M., Structure and function of plant cell wall proteins. Plant Cell, 5, 9–23 (1993).
  • 24) Danhash, N., Wagemakers, C. A., van Kan, J. A., and de Wit, P. J., Molecular characterization of four chitinase cDNAs obtained from Cladosporium fulvum-infected tomato. Plant Mol. Biol., 22, 1017–1029 (1993).
  • 25) Van Damme, E. J., Barre, A., Rouge, P., and Peumans, W. J., Potato lectin: an updated model of a unique chimeric plant protein. Plant J., 37, 34–45 (2004).
  • 26) Wright, C. S., Crystal structure of a wheat germ agglutinin/glycophorin-sialoglycopeptide receptor complex. Structural basis for cooperative lectin-cell binding. J. Biol. Chem., 267, 14345–14352 (1992).
  • 27) Harata, K., and Muraki, M., Crystal structures of Urtica dioica agglutinin and its complex with tri-N-acetylchitotriose. J. Mol. Biol., 297, 673–681 (2000).
  • 28) Edge, A. S., Deglycosylation of glycoproteins with trifluoromethanesulphonic acid: elucidation of molecular structure and function. Biochem. J., 376, 339–350 (2003).
  • 29) Desai, N. N., Allen, A. K., and Neuberger, A., The properties of potato (Solanum tuberosum) lectin after deglycosylation by trifluoromethanesulphonic acid. Biochem. J., 211, 273–276 (1983).
  • 30) Van Holst, G. J., and Varner, J. E., Reinforced polyproline II conformation in a hydroxyproline-rich cell wall glycoprotein from carrot root. Plant Physiol., 74, 247–251 (1984).
  • 31) Stafstrom, J. P., and Staehelin, L. A., The role of carbohydrate in maintaining extensin in an extended conformation. Plant Physiol., 81, 242–246 (1986).
  • 32) Vuorela, A., Myllyharju, J., Nisshi, R., Pihlajaniemi, T., and Kivirikko, K. I., Assembly of human prolyl 4-hydroxylase and type III collagen in the yeast Pichia pastoris: formation of a stable enzyme tetramer requires coexpression with collagen and assembly of stable collagen requires coexpression with prolyl 4-hydroxylase. EMBO J., 16, 6702–6712 (1997).
  • 33) Goto, M., Protein O-glycosylation in fungi: diverse structures and multiple functions. Biosci. Biotechnol. Biochem., 71, 1415–1427 (2007).
  • 34) Kawashima, H., Sueyoshi, S., Li, H., Yamamoto, K., and Osawa, T., Carbohydrate binding specificities of several poly-N-acetyllactosamine-binding lectins. Glycoconj. J., 7, 323–334 (1990).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.