Purification and structural characterization of lectins from the cnidarian Bunodeopsis antillienis

• Published in: Toxicon (Oxford) 2003-10, Vol.42 (5), p.525-532
• Main Authors: Fenton-Navarro, Bertha, Arreguı́n-L, Barbarı́n, Garcı́a-Hernández, Enrique, Heimer, Edgar, B. Aguilar, Manuel, Rodrı́guez-A, Claudia, Arreguı́n-Espinosa, Roberto
• Format: Article
• Language: English
• Subjects: Agglutinins; Anemone; Animal poisons toxicology. Antivenoms; Biological and medical sciences; Cnidarian; Lectins; Medical sciences; Toxicology
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/S0041-0101(03)00231-9

Purification and characterization of two different lectins from the Mexican anemone Bunodeopsis antillienis are reported. These two lectins named Bunodeopsis antillienis agglutinin-A (BAA-A) and -B (BAA-B) presented the following characteristics: BAA-A was resolved as a component, with haemagglutinating activity for human blood type A (N-acetylgalactosamine–galactose–fucose), with a molecular weight of 28,900 obtained by means of mass spectrometry, showed an isoelectric point of 5.04 with a higher carbohydrate specificity for N-acetylgalactosamine (GalNAc). The analysis of the N-terminal revealed it is related to phosphoesterase and GTP binding protein. BAA-B mainly active with human blood type B (galactose–galactose–fucose) was resolved into three fractions (BAA-B1-3). Their molecular weight were: BAA-B(1) 39,350, BAA-B(2) 28,300 and BAA-B(3) 17,550. The estimated isoelectric points were 8.05, 4.66 and 6.60, respectively. Only fraction 3 exhibited haemagglutinating activity with a higher carbohydrate specificity for galactose and mannose. The analysis of the N-terminal pointed out it is related with phospholipase A2. We suggest these lectins could be related to a feeding strategy.