Author(s): GilboaGarber N, Sudakevitz D
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Abstract The two Pseudomonas aeruginosa lectins PA-IL and PA-IIL, which are very similar in subunit size, composition and properties, but differ in carbohydrate specificity, were shown to exhibit opposite temperature profiles in hemagglutination tests. The galactophilic PA-IL, which interacts with the erythrocyte I antigen (together with B or P system antigens), resembles Ii system-specific 'cold hemagglutinins' (including antibodies and lectins of animals and plants) in low (4 degrees C) temperature optimum, while the hemagglutination by the fucose- and mannose-binding PA-IIL (like that of antibodies and lectins which do not bind to these antigens) increases on raising the temperature from 4 to 37 degrees C and even to 42 degrees C. The preferential production of both P. aeruginosa lectins at 28 degrees C and their much stronger interaction with enzyme (protease or sialidase)-damaged cells, as well as the lower temperature optimum (4 degrees C) of PA-IL-binding to the host cells, may be associated with the saprophytic rather than parasitic designation of this bacterium.
This article was published in FEMS Immunol Med Microbiol
and referenced in Journal of Glycomics & Lipidomics