Isolation and characterization of a Forssman antigen-binding lectin from velvet bean ( Mucuna derringiana ) seeds

A Forssman antigen (GalNAcα1-3GalNAcβ1-3Galα1-4Galβ1-4Glcβ1-1Cer)-binding lectin has been purified from velvet bean ( Mucuna derringiana ) seeds by a combination of affinity chromatography and reversed phase HPLC. This lectin agglutinates both native and trypsin-treated sheep erythrocytes as well as trypsinized rabbit erythrocytes, but neither native rabbit nor human erythrocytes, irrespective of blood group type. SDS-PAGE and gel filtration chromatography reveal the lectin to be a homodimer consisting of two 54 kDa subunits linked by non-covalent bonds. The results obtained by quantitative precipitation, haemagglutination inhibition and TLC overlay assays indicate that the Mucuna lectin specifically recognizes Forssman antigen and Forssman disaccharide (GalNAcα1-3GalNAc)-related structures.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/45669/1/10719_2004_Article_BF00731278.pd

Plant lectins: the ties that bind in root symbiosis and plant defense

Lectins are a diverse group of carbohydrate-binding proteins that are found within and associated with organisms from all kingdoms of life. Several different classes of plant lectins serve a diverse array of functions. The most prominent of these include participation in plant defense against predators and pathogens and involvement in symbiotic interactions between host plants and symbiotic microbes, including mycorrhizal fungi and nitrogen-fixing rhizobia. Extensive biological, biochemical, and molecular studies have shed light on the functions of plant lectins, and a plethora of uncharacterized lectin genes are being revealed at the genomic scale, suggesting unexplored and novel diversity in plant lectin structure and function. Integration of the results from these different types of research is beginning to yield a more detailed understanding of the function of lectins in symbiosis, defense, and plant biology in general