Expression of jumper ant (Myrmecia pilosula) venom allergens: post-translational processing of allergen gene products.
N-terminal analyses of electrophoretically-separated allergenic polypeptides of the venom of the jumper ant M. pilosula showed that five out of the six allergenic polypeptides identified are homologous with the cloned major allergen Myr p I and may be derived from a single precursor polypeptide. The sixth polypeptide is homologous with a second cloned major allergen, Myr p II which is expressed as a single precursor polypeptide but exists in its native form as a disulphide bond-linked complex.
Donovan
G R
GR
Molecular Immunology Unit, Kolling Institute of Medical Research, Royal North Shore Hospital, St. Leonards NSW, Australia.
Street
M D
MD
Tetaz
T
T
Smith
A I
AI
Alewood
D
D
Alewood
P
P
Sutherland
S K
SK
Baldo
B A
BA
D000478:Alkylation; D000485:Allergens; D000595:Amino Acid Sequence; D000818:Animals; D000862:Ant Venoms / Q000737:chemistry* / Q000235:genetics* / Q000276:immunology; D001000:Ants / Q000235:genetics*; D018076:DNA, Complementary / Q000276:immunology; D004220:Disulfides / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D015151:Immunoblotting; D019476:Insect Proteins; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011498:Protein Precursors / Q000235:genetics / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid
D000485:Allergens; D000862:Ant Venoms; D018076:DNA, Complementary; D004220:Disulfides; D019476:Insect Proteins; C079435:Myr p I; C096132:Myr p II protein, Myrmecia pilosula; D011498:Protein Precursors