The isolation and characterization of a novel collagenolytic serine protease allergen (Der p 9) from the dust mite Dermatophagoides pteronyssinus

King, C; Simpson, RJ; Moritz, RL; Reed, GE; Thompson, PJ; Stewart, GA

Author(s): King, C; Simpson, RJ; Moritz, RL; Reed, GE; Thompson, PJ; Stewart, GA;
Details: Publication Year 1996-10,Volume 98,Issue #4,Page 739-747
Journal Title: JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY
Publication Type: Journal Article
Abstract: Background: Dust mites have been shown to contain a serine protease distinct from the previously reported trypsin and chymotrypsin. The latter enzymes have been shown to be allergens, but the allergenic importance of the former is unknown. Objective: This study was performed to isolate and characterize the novel mite serine protease and determine its allergenicity. Methods: The mire serine protease was isolated from feces-enriched extracts of Dermatophagoides pteronyssinus by ion-exchange chromatography and affinity chromatography, and its physicochemical properties were determined The allergenicity of the protease was assessed by using the RAST. Results: The protease was enzymatically similar to chymotrypsin and cathepsin G-like enzymes from a variety of sources and was shown to cleave collagen. It had a molecular mass of 23,780 d. N-terminal sequence analysis (18 residues) indicated homology with the mite tryptic allergen Der p 3, and the chymotryptic allergen Der p 6. RAST analyses showed that the frequencies of reactivity to the novel allergen and to Der p 1, Der p 2, Der p 3, and Der p 6 were 92%, 97%, 100% 97%, and 65%, respectively (n = 35). RAST inhibition studies showed some cross-reactivity between the protease and Der p 3 but not Der p 6. Conclusions: A novel mite serine protease was isolated from D. pteronyssinus and found to be a major allergen. This allergen has been tentatively designated Der p 9.
Publisher: MOSBY-YEAR BOOK INC
Keywords: GROUP-III ALLERGEN; SEQUENCE-ANALYSIS; PHYSICOCHEMICAL CHARACTERIZATION; LIQUID-CHROMATOGRAPHY; SUBSTRATE; ENZYMES; HEPATOPANCREAS; PURIFICATION; SPECIFICITY; ELASTASE
Publisher's Version: https://doi.org/10.1016/S0091-6749(96)70121-5
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 1996-10-01 12:00:00