Molecular cloning and characterization of a major allergen (Myr p I) from the venom of the Australian jumper ant, Myrmecia pilosula.
Five IgE-binding components were identified in the venom of the Australian jumper ant, Myrmecia pilosula using SDS polyacrylamide gel electrophoresis and Western blotting. A cDNA clone which encodes the entire amino acid sequence of one of the major IgE-binding venom allergens has been nucleotide sequenced. The IgE-binding determinants of this allergen are located in its C-terminal domain. Database searches, however, did not reveal any homology with any other known nucleotide or protein sequence. The sequenced allergenic polypeptide has, according to the convention recommended by the International Union of Immunological Societies (IUIS), been named Myr p I.
Donovan
G R
GR
Kolling Institute of Medical Research, Royal North Shore Hospital, St. Leonards, Australia.
Baldo
B A
BA
Sutherland
S
S
D000485:Allergens / Q000096:biosynthesis* / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D000862:Ant Venoms; D001180:Arthropod Venoms / Q000096:biosynthesis* / Q000737:chemistry* / Q000276:immunology; D001315:Australia; D001483:Base Sequence; D003001:Cloning, Molecular; D004262:DNA Restriction Enzymes; D000939:Epitopes; D016678:Genome; D006801:Humans; D006927:Hymenoptera; D007073:Immunoglobulin E / Q000276:immunology / Q000302:isolation & purification; D008969:Molecular Sequence Data
D000485:Allergens; D000862:Ant Venoms; D001180:Arthropod Venoms; D000939:Epitopes; C079435:Myr p I; D007073:Immunoglobulin E; D004262:DNA Restriction Enzymes