Allergens in Hymenoptera venom. XVI: Studies of the structures and cross-reactivities of vespid venom phospholipases.
Phospholipases (PLs) isolated from the venoms of three species of yellow jackets, white-faced hornets, European hornets, and paper wasps were studied by peptide mapping after limited enzyme hydrolyses and cyanogen bromide cleavage. Significant differences in the primary structures were observed. Cross-reactivities of vespid PLs were studied by precipitation reactions in gel with rabbit antibodies, immunoblots of sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels with rabbit antisera, and RAST inhibition with individual sera from vespid-reactive patients. The cross-reactivities of both human IgE antibodies and rabbit IgG antibodies were variable and not reciprocal between antigen and antibody, suggesting that there are multiple antigenic determinants on the PL molecules and that individuals respond to different determinants. No general patterns of cross-reactivity could be observed.
D000485:Allergens / Q000032:analysis*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001514:Bee Venoms / Q000276:immunology*; D003429:Cross Reactions; D006801:Humans; D006927:Hymenoptera / Q000276:immunology*; D008245:Lysophospholipase / Q000032:analysis; D010446:Peptide Fragments / Q000032:analysis; D010740:Phospholipases / Q000032:analysis* / Q000276:immunology; D010741:Phospholipases A / Q000032:analysis; D011852:Radioallergosorbent Test; D013045:Species Specificity; D014862:Wasp Venoms / Q000276:immunology*; D014863:Wasps / Q000032:analysis / Q000276:immunology*
D000485:Allergens; D000596:Amino Acids; D001514:Bee Venoms; D010446:Peptide Fragments; D014862:Wasp Venoms; D010740:Phospholipases; D010741:Phospholipases A; D008245:Lysophospholipase