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Glycobiology Advance Access published online on May 24, 2006
Glycobiology, doi:10.1093/glycob/cwl006
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received December 24, 2005
Revised May 10, 2006
Accepted May 21, 2006

Article

LysM domains of Medicago truncatula NFP protein involved in Nod factor perception. Glycosylation state, molecular modeling and docking of chitooligosaccharides and Nod factors

Lonneke Mulder 1, Benoît Lefebvre 1, Julie Cullimore 1, and Anne Imberty 2 *

1 Laboratoire des Interactions Plantes-Microorganismes, INRA-CNRS, BP 52627, 31326 Castanet-Tolosan cedex, France
2 Centre de Recherches sur les Macromolécules Végétales, CNRS (affiliated with Université Joseph Fourier), BP 53, 38041 Grenoble cedex 9, France

* To whom correspondence should be addressed.
Anne Imberty, E-mail: imberty{at}cermav.cnrs.fr


  Abstract

The establishment of the symbiosis between legume plants and rhizobial bacteria depends on the production of rhizobial lipo-chitooligosaccharidic signals (the Nod factors), that are specifically recognized by roots of the host plant. In Medicago truncatula, specific recognition of Sinorhizobium meliloti and its Nod factors, requires the NFP (Nod Factor Perception) gene, which encodes a putative serine/threonine receptor-like-kinase. The extracellular domain of this protein contains three tandem Lysin motifs (LysM), a short peptide domain that is implicated in peptidoglycan or chitin binding in various bacterial and eukaryotic proteins respectively. We report here the homology modeling of the three LysM domains of M. truncatula NFP based on the structure of a LysM domain of the Escherichia coli membrane-bound lytic murein transglycosidase D (MltD). Expression of NFP in a homologous system (M. truncatula roots) revealed that the protein is highly N-glycosylated, probably with both high-mannose and complex glycans. Surface analysis and docking calculations performed on the models of the three domains were used to predict the most favored binding modes for chito-oligosaccharides and Nod factors. A convergent model can be proposed where the sulfated, O-acetylated lipo-chitooligosaccharidic Nod factor of S. meliloti binds in similar orientation on the three LysM domains of M. truncatula NFP. N-glycosylation is not expected to interfere with Nod factor binding in this orientation.

Keywords: LysM/Rhizobium/Nod factors/molecular modeling.
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