Lack of lysozyme activity of natural and yeast-derived recombinant Der p 2.
For Dermatophagoides pteronyssinus a number of allergens have been reported. Although the function of several allergens is known, that of the house dust mite allergen Der p 2 is unknown. A role as lysozyme has been suggested. We tested a yeast-derived recombinant Der p 2 for its lysozymatic activity. This recombinant allergen and affinity-purified natural Der p 2 lacked this enzymatic activity. Whole-body mite extract retained its lysozymatic activity after removal of the group 2 allergen by monoclonal antibody depletion. Analysis of spent medium revealed the reciprocal: it contained group 2 allergen, but lacked lysozymatic activity. Together, these data demonstrate that mite lysozyme and Der p 2 are different components of mite extract.
Hakkaart
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GA
Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, University of Amsterdam, The Netherlands.
Aalberse
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RC
van Ree
R
R
D000485:Allergens / Q000737:chemistry* / Q000235:genetics; D000818:Animals; D039741:Antigens, Dermatophagoides; D006023:Glycoproteins / Q000737:chemistry* / Q000235:genetics; D008925:Mites / Q000276:immunology*; D009113:Muramidase / Q000032:analysis*; D011994:Recombinant Proteins / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000235:genetics
D000485:Allergens; D039741:Antigens, Dermatophagoides; D006023:Glycoproteins; D011994:Recombinant Proteins; D009113:Muramidase