Purification and characterization of a D‐mannose specific lectin from the green marine alga, Bryopsis plumosa

Abstract

A D-mannose specific lectin was purified from the green marine alga, Bryopsis plumosa (Huds.) Ag. The lectin agglutinated horse and sheep erythrocytes. Matrix assisted laser desorption/ionization time of flight mass spectrometry, size exclusion chromatography, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and two dimensional gel electrophoresis (2DE) results showed that the lectin was a monomer with molecular weight of 17 kDa and pI 7.3. The agglutinating activity was inhibited by D-mannose (1 mM), a-methyl-D-mannose (4 mM) and L-fucose (8 mM). D-glucose (125 mM) showed weak inhibition. The lectin did not need divalent cations for agglutinating activity. N-terminal amino acid sequence of the lectin was analyzed. As the lectin was novel, we named it BPL-2 (Bryopsis plumosa lectin 2). Full cDNA sequence of BPL-2 was obtained using cDNA library. It was comprised of 624 bp of open reading frame and 167 bp/ 57 bp of 3′/5′ untranslated regions as well as N-terminal signal peptide. No antimicrobial activity of BPL-2 was observed in four bacteria strains tested.

Purification and characterization of a lectin, BPL-3, from the marine green alga Bryopsis plumosa

“…For the successful aggregation of cell organelles during protoplast formation of B. plumosa, the existence of additional lectin/s has been suggested, which may function similar to Bryohealin (Kim et al 2001Han et al 2010). Here, we describe the biochemical and molecular characterization of the third unique lectin from B. plumosa, BPL-3.…”

“…When N-acetyl-D-galactosamine was added to the column first, both lectins were eluted continuously, which made it difficult to isolate two lectins separately (data not shown). When we used N-acetyl-D-glucosamine affinity chromatography instead of N-acetyl-D-galactosamine column, Bryohealin came out first with treatment of N-acetyl-D-glucosamine and most of BPL-3 was retained in the column even with the treatment of 0.5 M N-acetyl-D-glucosamine Han et al 2010).…”

Effects of Plant Lectins on Human Erythrocyte Agglutination

“…These proteins are widely distributed in living organisms such as algae, animals, microorganisms, fungi and plants (5)(6)(7). Plant lectins have mostly been found in seeds and in almost all types of vegetative tissues, including fruits, bulbs, leaves, stems and roots (8)(9)(10)(11).…”

Isolation, Partial Purification and Characterization of Texas Live Oak (<i>Quercus fusiformis</i>) Lectin

“…Artocarpus incisa seed lectin resulted in non-blood group specificity in humans ABO system, while rabbit blood group activity was not different from human ABO and the other four blood groups were significantly different from human and rabbit agglutination [54]. Similarly, Bryopsis plumosa lectin from a green marine alga agglutinated sheep and horse erythrocytes [55]. The blood group specificity of Q. fusiformis lectin activity suggests Q. fusiformis lectin is non-blood group specific with higher specificity directed towards sheep erythrocytes.…”