Identification of an IgE-binding determinant of the major allergen Myr p I from the venom of the Australian jumper ant Myrmecia pilosula.
The structure of the single allergenic determinant of the major ant venom allergen, Myr p I from the Australian jumper ant Myrmecia pilosula has been determined by inhibition studies with synthetic peptides. A 14 amino-acid C-terminal peptide sequence has been shown to constitute this determinant. Half-maximal inhibition of binding of ant venom-specific IgE antibodies to the native venom was obtained with this peptide at a concentration of 5 x 10(-8) M. This allergenic determinant was invariant for all ant venom-allergic subjects tested whose IgE antibodies recognized this allergen.
Donovan
G R
GR
Kolling Institute of Medical Research, Royal North Shore Hospital, St. Leonards, NSW, Australia.
Street
M D
MD
Baldo
B A
BA
Alewood
D
D
Alewood
P
P
Sutherland
S
S
D000485:Allergens / Q000737:chemistry*; D000595:Amino Acid Sequence; D000862:Ant Venoms / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000276:immunology; D001180:Arthropod Venoms / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000276:immunology; D001667:Binding, Competitive; D000939:Epitopes / Q000737:chemistry* / Q000276:immunology; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology*; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000276:immunology; D011863:Radioimmunoassay
D000485:Allergens; D000862:Ant Venoms; D001180:Arthropod Venoms; D000939:Epitopes; C079435:Myr p I; D010455:Peptides; D007073:Immunoglobulin E