Purification of a lectin from the marine red alga Gracilaria cornea and its effects on the cattle tick Boophilus microplus (Acari: Ixodidae)

A lectin was purified from the seaweed Gracilaria cornea by hydrophobic interaction chromatography on phenyl-Sepharose CL-4B followed by affinity chromatography on immobilized mucin. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of G. cornea lectin (GCL) revealed a single protein band of approximately 60 kDa, whereas by gel filtration on Sephadex G-100 its native molecular mass was 66 kDa. GCL exhibited a single isoeletric point of 4.3 and a 52.5% content of neutral sugars. Furthermore, the EDTA-treated lectin did not show any significant decrease in its ability to agglutinate trypsin-treated chicken erythrocytes. These data suggest that GCL is an acidic, monomeric glycoprotein that probably does not require divalent metal ions for its hemagglutinating activity. GCL hemagglutinating activity was not inhibited by any of the mono-, di-, and trisaccharides tested but was by the complex glycoproteins fetuin and porcine stomach mucin. Exposure of engorged females of the cattle tick (Boophilus microplus) to 0.1 mg mL(-1) GCL significantly (P < 0.05) reduced the female weight after the oviposition period, the egg mass weight, the hatching period, and the mean larvae survival time.