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First published online October 13, 2006; 10.1104/pp.106.087437 Plant Physiology 144:637-647 (2007) © 2007 American Society of Plant Biologists OPEN ACCESS ARTICLE
The Liverwort Marchantia polymorpha Expresses Orthologs of the Fungal Agaricus bisporus Agglutinin Family1,[W],[OA]Nievelveldweg 9, B9310 Aalst, Belgium (W.J.P.); Department of Molecular Biotechnology, Laboratory of Biochemistry and Glycobiology (E.F., N.L., E.J.M.V.D.) and Laboratory for Protein Biochemistry and Protein Engineering (B.D.), Ghent University, 9000 Ghent, Belgium; l'Institut Fédératif de Recherche 40-Centre National de la Recherche Scientifique, Signalisation et Biotechnologie Végétales, 31326 Castanet Tolosan, France (A.J.); Surfaces Cellulaires et Signalisation chez les Végétaux, Unité Mixte de la Recherche, Centre National de la Recherche Scientifique-Université Paul Sabatier 5546, Pôle de Biotechnologies Végétales, 31326 Castanet-Tolosan, France (P.R.); Department of Applied Science, Okayama University of Science, Okayama 7000005, Japan (H.H.); and Department of Biochemistry and Molecular Biology, University of Oklahoma, Health Sciences Center, Oklahoma City, Oklahoma (R.A.)
A lectin different from the previously described mannose-binding agglutinins has been isolated from the liverwort Marchantia polymorpha. Biochemical characterization of the purified lectin combined with the data from earlier transcriptome analyses demonstrated that the novel M. polymorpha agglutinin is not related to any of the known plant lectin families, but closely resembles the Agaricus bisporus-type lectins, which hitherto have been found exclusively in fungi. Immunolocalization studies confirmed that lectin is exclusively associated with plant cells, ruling out the possibility of a fungal origin. Extensive screening of publicly accessible databases confirmed that, apart from fungi, the occurrence of A. bisporus-type lectins is confined to M. polymorpha and the moss Tortula ruralis. Expression of a typical fungal protein in a liverwort and a moss raises the question of the origin of the corresponding genes. Regardless of the evolutionary origin, the presence of a functional A. bisporus lectin ortholog in M. polymorpha provides evidence for the expression of an additional carbohydrate-binding domain in Viridiplantae.
1 This work was supported by the Fund for Scientific Research-Flanders (project no. G.0201.04) and the Research Council of Ghent University. The glycan array analysis was conducted by the Protein-Glycan Interaction Core H of the Consortium for Functional Glycomics funded by the National Institute of General Medical Sciences (grant no. GM62116). The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instruction for Authors (www.plantphysiol.org) is: Els J.M. Van Damme (elsjm.vandamme{at}ugent.be). [W] The online version of this article contains Web-only data. [OA] Open Access articles can be viewed online without a subscription. www.plantphysiol.org/cgi/doi/10.1104/pp.106.087437 * Corresponding author; e-mail elsjm.vandamme{at}ugent.be; fax 3292646219. Received July 27, 2006; accepted September 24, 2006; published October 13, 2006. This article has been cited by other articles:
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