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IgE binding studies with large peptides expressed from Der p II cDNA constructs
Journal article   Peer reviewed

IgE binding studies with large peptides expressed from Der p II cDNA constructs

K-Y Chua, W.K. Greene, P. Kehal and W.R. Thomas
Clinical & Experimental Allergy, Vol.21(2), pp.161-166
1991
DOI: https://doi.org/10.1111/j.1365-2222.1991.tb00825.x
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Abstract

The major mite allergen Der p II shows marked resistance to denaturation and is expressed from cDNA in bacteria with almost all of its IgE binding activity. Despite these properties, the IgE binding activity appears to be dependent on maintaining the complete primary structure. Random fragment libraries of cDN A, able to code for up to 93 of the 129 amino acid residue protein, did not express IgE binding peptides. Large overlapping peptides 1–69, 69–129 and 42–117 expressed as the fusions from the glutathione transferase of pGEX vectors only had binding activity with IgE in 15 out of 57 sera, and this was typically weak. Sera from children with atopic dermatitis bound IgE in seven out of eight cases but this was also weak compared with their strong reactivity to intact recombinant Der p II. The inability of such large peptides to form IgE binding structures suggests that the antigenic determinants of Der p II are highly conformational and restricted.

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Source: InCites

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Collaboration types
Domestic collaboration
Citation topics
1 Clinical & Life Sciences
1.65 Allergy
1.65.264 Allergy Mechanisms
Web Of Science research areas
Allergy
Immunology
ESI research areas
Immunology
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