Structural studies of a hornet venom allergen antigen 5, Dol m V and its sequence similarity with other proteins.
The primary structures and the disulfide-bond pairings of two chromatographic forms A and B of a venom protein from white-faced hornet (Dolichovespula maculata) were determined. This protein, designated as antigen 5 (Dol m V), has 204-205 amino acid residues and it contains 4 disulfide bonds. This protein is an allergen in man but its biologic function in hornet is not yet known. Dol m V is found to have partial sequence similarity with pathogenesis-related proteins from tobacco and tomato leaves and with a sperm-coating protein from rat epididymis.
Rockefeller University, New York, NY 10021-6399.
T P
TP
King
D
D
Moran
D F
DF
Wang
L
L
Kochoumian
B T
BT
Chait
D000595:Amino Acid Sequence; D000818:Animals; D000941:Antigens / Q000032:analysis*; D001514:Bee Venoms / Q000032:analysis*; D003429:Cross Reactions; D004220:Disulfides / Q000032:analysis; D006801:Humans; D006927:Hymenoptera / Q000276:immunology*; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D014862:Wasp Venoms / Q000032:analysis*; D014863:Wasps / Q000276:immunology*
D000941:Antigens; D001514:Bee Venoms; D004220:Disulfides; D014862:Wasp Venoms; C040583:white-faced hornet venom antigen 5