Mannose-binding hemagglutinins in extracts of Pseudomonas aeruginosa

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Abstract
Mannose-binding hemagglutinins were found in the extracts of a pyocyanin-forming P. aeruginosa, which contain galactose-specific hemagglutinins. They were purified simultaneously with the latter proteins by heating to 70.degree. C, precipitating with (NH4)2SO4, application to a Sepharose 4B column and elution from it by 0.05 M mannose. The mannose-specific hemagglutinins were similar to the galactophilic ones in being glycoproteins of very low MW (about 11,000 by SDS [sodium dodecyl sulfate] gel electrophoresis), their tendency to aggregate and their ability to effect stronger agglutination of erythrocytes treated with papain than of untreated ones. They resembled them also in their reaction with simple sugars and interactions with divalent cations, which are essential for their activity. In these properties, and in their relative resistance to heat and to proteolytic enzymes, these 2 types of bacterial hemagglutinins are like most of the plant, contrasted with the animal, hemagglutinins. The reactions with mannose and mannose-bearing compounds (yeast mannan, horseradish peroxidase (EC 1.11.1.7) and serum globulins), which are not shared with the galactophilic Pseudomonas hemagglutinins, indicate a relationship of the mannose-binding protein of Pseudomonas to the plant lectin concanavalin A. The mannose-binding hemagglutinins do not exhibit identical cell-agglutinating spectra owing to difference in profiles of sugar specificity and relative affinity to mannose derivatives compared with free mannose.