Demonstration of a partially cryptic epitope of the major cat allergen Fel d 1: consequences for mAb-based standardization of cat extracts.

作者: Thierry Batard , Fidélia Bukovec , Christelle Berrouet , Véronique Destombes , Alain Didierlaurent

DOI: 10.1067/MAI.2000.110227

关键词:

摘要: Abstract Background: Antiallergen mAbs that do not recognize clinically important isoforms have been described, raising the question of selection for quantifying major allergens in order to standardize allergenic extracts. This is even more critical if can discriminate between different forms allergen molecules with same amino acid sequence. Objective: We sought demonstrate an anti-Fel d 1 mAb was able two cat independently its sequence and determine relative importance stability both various Methods: Anti-Fel were raised mice characterized. By using these mAbs, a two-site ELISA developed quantify Fel mass units. Results: One shown specifically particular form 1. A this capture form. It then (1) quantitative could vary from one extract another, (2) converted into under certain conditions, (3) unconverted may bear IgE epitopes are specific. Conclusion: Although present study emphasizes issue selecting too specific extracts, it also demonstrates very be interest, especially verify since might clinical implications. (J Allergy Clin Immunol 2000;106:669-76.)

参考文章(9)
C. Korth, B. Stierli, P. Streit, M. Moser, O. Schaller, R. Fischer, W. Schulz-Schaeffer, H. Kretzschmar, A. Raeber, U. Braun, F. Ehrensperger, S. Hornemann, R. Glockshuber, R. Riek, M. Billeter, K. Wüthrich, B. Oesch, Prion (PrPSc)-specific epitope defined by a monoclonal antibody Nature. ,vol. 390, pp. 74- 77 ,(1997) , 10.1038/36337
Oscar A. Duffort, José Carreira, Gianpaolo Nitti, Florentino Polo, Manuel Lombardero, Studies on the biochemical structure of the major cat allergen Felis domesticus I Molecular Immunology. ,vol. 28, pp. 301- 309 ,(1991) , 10.1016/0161-5890(91)90141-6
Florine J. van Milligen, Peter van Swieten, Rob C. Aalberse, Structure of the major cat allergen Fel d I in different allergen sources: an immunoblotting analysis with monoclonal antibodies against denatured Fel d I and human IgE. International Archives of Allergy and Immunology. ,vol. 99, pp. 63- 73 ,(1992) , 10.1159/000236337
A. DORNELAS DE ANDRADE, J. BIRNBAUM, C. MAGALON, J. P. MAGNOL, A. LANTEAUME, D. CHARPIN, D. VERVLOET, Fel d I levels in cat anal glands Clinical & Experimental Allergy. ,vol. 26, pp. 178- 180 ,(1996) , 10.1111/J.1365-2222.1996.TB00077.X
H DEGROOT, P VANSWIETEN, J VANLEEUWEN, P LIND, R AALBERSE, Monoclonal antibodies to the major feline allergen Fel d I: I. Serologic and biologic activity of affinity-purified Fel d I and of Fel d I-depleted extract The Journal of Allergy and Clinical Immunology. ,vol. 82, pp. 778- 786 ,(1988) , 10.1016/0091-6749(88)90079-6
G. KÖHLER, C. MILSTEIN, Continuous cultures of fused cells secreting antibody of predefined specificity Nature. ,vol. 256, pp. 495- 497 ,(1975) , 10.1038/256495A0
G. A. J. Hakkaart, M. D. Chapman, R. C. Aalberse, R. Van Ree, Immune-reactivity of recombinant isoforms of the major house dust mite allergen Der p 2 Clinical & Experimental Allergy. ,vol. 28, pp. 169- 174 ,(1998) , 10.1046/J.1365-2222.1998.00205.X