Polyphemin: a teichoic acid-binding lectin from the horseshoe crab, Limulus Polyphemus.
A Staphylococcus aureus-agglutinating lectin, capable of binding to N-acetyl-D-glucosamine, was isolated from the serum of Limulus polyphemus. The monosaccharide alone was incapable of inhibiting bacterial agglutination by this lectin. Quantitative precipitation studies with purified cell wall-derived teichoic acids, either devoid of or containing N-acetyl-D-glucosamine, confirmed the carbohydrate-binding specificity of the lectin and suggested that secondary, non-specific interactions contribute to binding biomolecules containing this sugar. The agglutination pattern with various S. aureus strains having N-acetyl-D-glucosamine-associated teichoic acid, teichoic acid without this sugar, and no teichoic acid indicated that this cell wall component is not the sole binding site for the lectin on intact S. aureus cells. Affinity gel chromatography, using N-acetyl-D-glucosamine-associated teichoic acid as the specific absorbent, has been used to isolate this lectin from Limulus serum.
D000372:Agglutination Tests; D000818:Animals; D060829:Arthropod Proteins; D011232:Chemical Precipitation; D002846:Chromatography, Affinity; D006737:Horseshoe Crabs / Q000032:analysis*; D037102:Lectins / Q000302:isolation & purification*; D013682:Teichoic Acids / Q000032:analysis*
D060829:Arthropod Proteins; D037102:Lectins; D013682:Teichoic Acids; C038447:polyphemin, Limulus polyphemus