Structural studies on the allergen Der p1 from the house dust mite Dermatophagoides pteronyssinus: similarity with cysteine proteinases.
A major allergen (Der p1) has been purified to homogeneity from faecal particles from the house dust mite Dermatophagoides pteronyssinus. Reversed-phase microbore HPLC was employed to fractionate and purify a number of tryptic peptides generated from approximately 20 nmol of purified Der p1. N-Terminal amino acid sequence analyses were performed on the intact polypeptide and six tryptic peptides yielding 89 unique assignments; this corresponds to 40% of the molecule. These data are compared with the cDNA-deduced amino acid sequence of the Der p1 allergen. There is extensive similarity between the N-terminal amino acid sequence of Der p1 and the cysteine proteases actinidin and papain. A low Mr protein (approximately 17,000) was resolved from S-carboxymethyl Der p1 by gel-permeation chromatography. Edman degradation of the first 24 residues of this material revealed no similarity with Der p1. It is not clear whether this component is a low Mr disulfide-linked chain derived from Der p1 or represents an unidentified mite component.
Simpson
R J
RJ
Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research, Parkville, Victoria, Australia.
Nice
E C
EC
Moritz
R L
RL
Stewart
G A
GA
D000485:Allergens / Q000032:analysis; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D039741:Antigens, Dermatophagoides; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D003546:Cysteine Endopeptidases / Q000032:analysis; D008925:Mites / Q000032:analysis*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010206:Papain
D000485:Allergens; D000596:Amino Acids; D039741:Antigens, Dermatophagoides; D003546:Cysteine Endopeptidases; C018745:actinidain; D010206:Papain