Glycoconjugate Journal

, Volume 11, Issue 4, pp 321–332

The monomeric and dimeric mannose-binding proteins from the Orchidaceae speciesListera ovata andEpipactis helleborine: sequence homologies and differences in biological activities


  • Els J. M. van Damme
    • Laboratory for Phytopathology and Plant ProtectionKatholieke Universiteit Leuven
  • Jan Balzarini
    • Laboratory of Experimental ChemotherapyRega Institute for Medical Research
  • Koen Smeets
    • Laboratory for Phytopathology and Plant ProtectionKatholieke Universiteit Leuven
  • Fred van Leuven
    • Center for Human GeneticsKatholieke Universiteit Leuven
  • Willy J. Peumans
    • Laboratory for Phytopathology and Plant ProtectionKatholieke Universiteit Leuven
Special Lectins Issue

DOI: 10.1007/BF00731205

Cite this article as:
van Damme, E.J.M., Balzarini, J., Smeets, K. et al. Glycoconjugate J (1994) 11: 321. doi:10.1007/BF00731205


The Orchidaceae speciesListera ovata andEpipactis helleborine contain two types of mannose-binding proteins. Using a combination of affinity chromatography on mannose-Sepharose-4B and ion exchange chromatography on a Mono-S column eight different mannose-binding proteins were isolated from the leaves ofListera ovata. Whereas seven of these mannose-binding proteins have agglutination activity and occur as dimers composed of lectin subunits of 11–13 kDa, the eighth mannose-binding protein is a monomer of 14 kDa devoid of agglutination activity. Moreover, the monomeric mannose-binding protein does not react with an antiserum raised against the dimeric lectin and, in contrast to the lectins, is completely inactive when tested for antiretroviral activity against human immunodeficiency virus type 1 and type 2. Mannose-binding proteins with similar properties were also found in the leaves ofEpipactis helleborine. However, in contrast toListera only one lectin was found inEpipactis. Despite the obvious differences in molecular structure and biological activities molecular cloning of different mannose-binding proteins fromListera andEpipactis has shown that these proteins are related and some parts of the sequences show a high degree of sequence homology indicating that they have been conserved through evolution.


cDNA cloningEpipactislectinListeramannose-binding



Epipactis helleborine mannose-binding protein


Listera ovata mannose-binding protein

Copyright information

© Chapman & Hall 1994