Structure of IgE epitopes on a new 39-kD allergen molecule from the house dust mite, Dermatophagoides farinae.
Two IgE epitope sequences comprising Ser56-Pro-Val-Thr-Lys-Arg-Ala-Ser-Leu-Lys-Ile-Asp-Ser-Lys-Lys70 and Asp104-Val-Glu-Leu-Ser-Leu-Arg-Ser-Ser-Asp-Ile-Ala115 were identified by deletion analysis of the cDNA encoding a new 39-kD protein of mite allergen. A synthetic dodecapeptide corresponding to the latter epitope sequence functioned as a monovalent and mite-specific hapten. Replacement of each of the 12 amino acid residues with Gly, using site-directed mutagenesis, indicated that Arg110 may play a central role in IgE binding. However, the 8 allergic sera tested exhibited a wide variation in their amino acid residues required for reactivity to IgE in allergic sera.
Aki
T
T
Department of Fermentation Technology, Faculty of Engineering, Hiroshima University, Japan.
Ono
K
K
Hidaka
Y
Y
Shimonishi
Y
Y
Jyo
T
T
Wada
T
T
Yamashita
M
M
Shigeta
S
S
Murooka
Y
Y
Oka
S
S
D000485:Allergens / Q000276:immunology*; D000818:Animals; D039741:Antigens, Dermatophagoides; D000939:Epitopes; D006023:Glycoproteins / Q000276:immunology*; D007073:Immunoglobulin E / Q000276:immunology; D008925:Mites / Q000276:immunology*; D016297:Mutagenesis, Site-Directed; D011994:Recombinant Proteins / Q000276:immunology; D017384:Sequence Deletion; D013329:Structure-Activity Relationship
D000485:Allergens; D039741:Antigens, Dermatophagoides; D000939:Epitopes; D006023:Glycoproteins; D011994:Recombinant Proteins; D007073:Immunoglobulin E