Evidence for lectin activity of a plant receptor-like protein kinase by application of neoglycoproteins and bioinformatic algorithms

Evidence for lectin activity of a plant receptor-like protein kinase by application of... Detection of genes for putative receptor-like protein kinases, which contain an extracellular domain related to leguminous lectins, in plant genomes inspired the hypothesis that this part acts as sensor. Initial support for this concept came from proof for protein kinase activity. The next step, focusing on the protein of lombardy poplar ( Populus nigra var. italica ), is scrutiny for lectin activity. Consequently, we first pinpointed sets of high-scoring sequence pairs by extensive databank search. The calculations resulted in P -values in the range from 10 −14 to 10 −18 exclusively for leguminous lectins, the Pterocarpus angolensis agglutinin being frontrunner with P = 3 × 10 −18 and thus most suitable template for modeling. The superimposition of the two folds gave notable similarity in the region responsible for binding carbohydrate and Ca 2+ /Mn 2+ -ions. Binding activity toward carbohydrates was detected by assaying a panel of (neo)glycoproteins as polyvalent probes, especially for α- l -rhamnose and glycans of asialofetuin. It was strictly dependent on Ca 2+ -ions, enhanced by Mn 2+ -ions and reached a K D -value of 34.3 nM for the neoglycoprotein with rhamnose as ligand. These results give further research direction to define physiological ligands, plant/bacterial rhamnose-containing saccharides and rhamnose-mimetic glycans or peptides being potential candidates. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biochimica et Biophysica Acta (BBA) - General Subjects Elsevier

Evidence for lectin activity of a plant receptor-like protein kinase by application of neoglycoproteins and bioinformatic algorithms

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Publisher
Elsevier
Copyright
Copyright © 2005 Elsevier B.V.
ISSN
0304-4165
D.O.I.
10.1016/j.bbagen.2005.04.004
Publisher site
See Article on Publisher Site

Abstract

Detection of genes for putative receptor-like protein kinases, which contain an extracellular domain related to leguminous lectins, in plant genomes inspired the hypothesis that this part acts as sensor. Initial support for this concept came from proof for protein kinase activity. The next step, focusing on the protein of lombardy poplar ( Populus nigra var. italica ), is scrutiny for lectin activity. Consequently, we first pinpointed sets of high-scoring sequence pairs by extensive databank search. The calculations resulted in P -values in the range from 10 −14 to 10 −18 exclusively for leguminous lectins, the Pterocarpus angolensis agglutinin being frontrunner with P = 3 × 10 −18 and thus most suitable template for modeling. The superimposition of the two folds gave notable similarity in the region responsible for binding carbohydrate and Ca 2+ /Mn 2+ -ions. Binding activity toward carbohydrates was detected by assaying a panel of (neo)glycoproteins as polyvalent probes, especially for α- l -rhamnose and glycans of asialofetuin. It was strictly dependent on Ca 2+ -ions, enhanced by Mn 2+ -ions and reached a K D -value of 34.3 nM for the neoglycoprotein with rhamnose as ligand. These results give further research direction to define physiological ligands, plant/bacterial rhamnose-containing saccharides and rhamnose-mimetic glycans or peptides being potential candidates.

Journal

Biochimica et Biophysica Acta (BBA) - General SubjectsElsevier

Published: Sep 15, 2005

References

  • Lectin receptor kinases in plants
    Barre, A.; Hervé, C.; Lescure, B.; Rougé, R.
  • The information-storing potential of the sugar code
    Laine, R.A.
  • A receptor-like protein kinase with a lectin-like domain from lombardy poplar: gene expression in response to wounding and characterization of phosphorylation activity
    Nishiguchi, M.; Yoshida, K.; Sumizono, T.; Tazaki, K.
  • Neoglycoconjugates
    Lee, R.T.; Lee, Y.C.
  • The sugar code: functional lectinomics
    Gabius, H.-J.; André, S.; Kaltner, H.; Siebert, H.-C.
  • Principles of structures of animal and plant lectins
    Loris, R.
  • Human keratinocyte membrane lectins: characterization and modulation of their expression by cytokines
    Cerdan, D.; Grillon, C.; Monsigny, M.; Redziniak, G.; Kieda, C.
  • Ultraviolet rays induced expression of lectins on the surface of a squamous carcinoma keratinocyte cell line
    Condaminet, B.; Redziniak, G.; Monsigny, M.; Kieda, C.
  • Purification and characterization of a rhamnose-binding lectin with immunoenhancing activity from grass carp ( Ctenopharyngodon idellus ) ovaries
    Lam, Y.W.; Ng, T.B.
  • Pectin: cell biology and prospects for functional analysis
    Willats, W.G.T.; McCartney, L.; Mackie, W.; Knox, J.P.
  • Structural elucidation of the O-chain of the lipopolysaccharide from Xanthomonas campestris strain 8004
    Molinaro, A.; Silipo, A.; Lanzetta, R.; Newman, M.A.; Dow, J.M.; Parrilli, M.
  • Comparative analysis of structural properties of the C-type lectin-like domain (CTLD)
    Zelensky, A.N.; Gready, J.E.

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