Extensive homologies between lectins from non-leguminous plants

AbstractSequence studies were performed on lectins from two non-leguminous plants: rice and nettle. Extensive homologies were found between these two proteins and wheat germ agglutinin in support of the conservation of lectin sequences among non-leguminous plants. The number and positions of the cysteine residues were particularly well conserved suggesting a similar folding of the polypeptide chains

Effect of plant lectins on larval development of legume pod borer, Maruca vitrata

The legume pod‐borer Maruca vitrata (Fabricius), [Lepidoptera: Pyralidae] is a major constraint restricting increased cowpea production in tropical Africa and Asia. Since lectins are known to have insecticidal properties against several pests, a survey was undertaken to screen for the effects of 25 lectins from 15 plant families on the development of Maruca pod borer (MPB) larvae. The list included 8 galactose/N‐acetylgalactosamine‐, 7 mannose‐, 5 complex glycan‐, 2 sialic acid‐ and 3, N‐acetylglucosamine‐specific lectins. Feeding bioassays using artificial diet were carried out at 2% (w/w) topical levels. Although a total of 16 lectins had detrimental effects pertaining either to larval survival, weight, feeding inhibition, pupation, adult emergence and/or fecundity, only the Listera ovata agglutinin (LOA) (Orchidaceae) and Galanthus nivalis (Amaryllidaceae) agglutinin were effective against MPB larvae for all six parameters examined. Larval mortality and feeding inhibition caused by the most active lectin (LOA) was above 60%

Isolation and partial characterisation of galactosespecific lectins from African yam beans, Sphenostylis stenocarpa Harms

A new galactose-specific lectin was isolated from African yam bean (Sphenostyles stenocarpa Harms) by affinity chromatography on galactose-Sepharose 4B. SDS–PAGE analysis resulted in four polypeptide bands of approximately 27, 29, 32 and 34 kDa, respectively. Based on the analysis of carbohydrate content and native PAGE, it is likely that the Sphenostyles lectin is a tetrameric glycoprotein with Mr of approximately 122 kDa. N-terminal protein sequencing of purified lectins from four different Sphenostyles accessions shows that the four polypeptides have largely identical amino acid sequences. The sequences contain the conserved consensus sequence F-F–LILG characteristic of legume lectins, as well as Phaseolus vulgaris proteins in the arcelin-α-amylase inhibitor gene family. The lectin agglutinates both rabbit and human erythrocytes, but with a preference for blood types A and O. Using Western blotting, the lectin was shown to accumulate rapidly during seed development, but levels dropped slightly as seeds attained maturity. This is the first time a lectin has been purified from the genus Sphenostyles. The new lectin was assigned the abbreviation LECp.SphSte.se.Hga1