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Clinical Chemistry and Laboratory Medicine (CCLM)

Published in Association with the European Federation of Clinical Chemistry and Laboratory Medicine (EFLM)

Editor-in-Chief: Plebani, Mario

Ed. by Gillery, Philippe / Greaves, Ronda / Lackner, Karl J. / Lippi, Giuseppe / Melichar, Bohuslav / Payne, Deborah A. / Schlattmann, Peter


IMPACT FACTOR 2018: 3.638

CiteScore 2018: 2.44

SCImago Journal Rank (SJR) 2018: 1.191
Source Normalized Impact per Paper (SNIP) 2018: 1.205

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1437-4331
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Volume 55, Issue 2

Issues

An alternative inhibition method for determining cross-reactive allergens

Yvonne Schmidt-Hieltjes / Malgorzata Teodorowicz / Ad Jansen
  • Department of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, The Netherlands
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Gerco den Hartog / Lisette Elfvering-Berendsen / Nicolette W. de Jong / Huub F.J. Savelkoul / Janneke Ruinemans-Koerts
Published Online: 2016-07-30 | DOI: https://doi.org/10.1515/cclm-2016-0172

Abstract

Background:

Inhibition assays are an useful tool to identify the allergen of primary sensitization of cross-reactive allergens. Classical ELISA-based inhibition assays are limited by both the availability of commercial standardized allergen extracts and the experience and knowledge needed for making home-made extracts. Moreover the direct comparison of the inhibition ELISAs outcomes between different laboratories is difficult because of different sources of used allergen extracts and a number of methodological variations. Therefore, we propose a novel ImmunoCap (Phadia, Thermofisher Scientific) based immunoinhibition method with the use of commercially available Caps as the allergen source.

Methods:

The novel ImmunoCap based immunoinhibition method was developed and tested with sera from patients with a well-known cross-reactive sensitization for fig (Ficus carica) and ficus (Ficus benjamina). Results were compared with a classically applied inhibition method, i.e. addition of homemade allergen extract to patient serum.

Results:

The amount of allergens (fig and ficus extracts) needed to reach a similar degree of inhibition was comparable for both inhibition methods.

Conclusions:

The ImmunoCap based inhibition assay, in addition to classical inhibition methods, is a valuable tool as the ImmunoCap analyzer and commercial allergens (Caps) are more widely available which makes the outcomes of inhibition tests comparable between different laboratories. Furthermore, in the ImmunoCap inhibition method the same protein source is used for both the inhibition of sIgE and sIgE measurement, which might be even more relevant when multiple cross-reactive allergens are tested.

Keywords: basophil activation test (BAT); cross-reactivity; ImmunoCap; immuno-inhibition

References

  • 1.

    Aalberse RC, Akkerdaas J, Van Ree R. Cross-reactivity of IgE antibodies to allergens. Allergy 2001;56:478–90.Google Scholar

  • 2.

    De Leon MP, Glaspole IN, Drew AC, Rolland JM, O’Hehir RE, Suphioglu C. Immunological analysis of allergenic cross-reactivity between peanut and tree nuts. Clin Exp Allergy 2003;33:1273–80.Google Scholar

  • 3.

    Guilloux L, Vuitton DA, Delbourg M, Lagier A, Adessi B, Marchand CR, et al. Cross-reactivity between terrestrial snails (Helix species) and house-dust mite (Dermatophagoides pteronyssinus). II. In vitro study. Allergy 1998;53:151–8.Google Scholar

  • 4.

    Focke M, Hemmer W, Wöhrl S, Götz M, Jarisch R. Cross-reactivity between Ficus benjamina latex and fig fruit in patients with clinical fig allergy. Clin Exp Allergy 2003;33:971–7.Google Scholar

  • 5.

    Maloney JM, Rudengren M, Ahlstedt S, Bock SA, Sampson HA. The use of serum-specific IgE measurements for the diagnosis of peanut, tree nut, and seed allergy. J Allergy Clin Immun 2008;122:145–51.Google Scholar

  • 6.

    Katial RK, Lin FL, Stafford WW, Ledoux RA, Westly CR, Weber RW. Mugwort and sage (Artemisia) pollen cross-reactivity: ELISA inhibition and immunoblot evaluation. Ann Allerg Asthma Immunol 1997;79:340–6.Google Scholar

  • 7.

    Sharp MF, Stephen JN, Kraft L, Weiss T, Kamath SD, Lopata AL. Immunological cross-reactivity between four distant parvalbumins – Impact on allergen detection and diagnostics. Mol Immunol 2015;63:437–48.Google Scholar

  • 8.

    Van Do T, Hordvik I, Endresen C, Elsayed S. The major allergen (parvalbumin) of codfish is encoded by at least two isotypic genes: cDNA cloning, expression and antibody binding of the recombinant allergens. Mol Immunol 2003;39:595–602.Google Scholar

  • 9.

    Moneret-Vautrin D-A, Guérin L, Kanny G, Flabbee J, Frémont S, Morisset M. Cross-allergenicity of peanut and lupine: The risk of lupine allergy in patients allergic to peanuts. J Allergy Clin Immunol 1999;104:883–8.Google Scholar

  • 10.

    Koppelman SJ, de Jong GA, Laaper-Ertmann M, Peeters KA, Knulst AC, Hefle SL, et al. Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: evidence for cross-reactivity with Ara h 2. Clin Exp Allergy 2005;35: 490–7.Google Scholar

  • 11.

    de Leon MP, Glaspole IN, Drew AC, Rolland JM, O’Hehir RE, Suphioglu C. Immunological analysis of allergenic cross-reactivity between peanut and tree nuts. Clin Exp Allergy 2003;33:1273–80.Google Scholar

  • 12.

    Goetz DW, Whisman BA, Goetz AD. Cross-reactivity among edible nuts: double immunodiffusion, crossed immunoelectrophoresis, and human specific IgE serologic surveys. Ann Allergy Asthma Immunol 2005;95:45–52.Google Scholar

  • 13.

    Teuber SS, Peterson WR. Systemic allergic reaction to coconut (Cocos nucifera) in 2 subjects with hypersensitivity to tree nut and demonstration of cross-reactivity to legumin-like seed storage proteins: New coconut and walnut food allergens. J Allergy Clin Immunol 1999;103:1180–5.Google Scholar

  • 14.

    Jung YG, Cho HJ, Park GY, Min JY, Kim HY, Dhong HJ, et al. Comparison of the skin-prick test and Phadia ImmunoCAP as tools to diagnose house-dust mite allergy. Am J Rhinol Allergy 2010;24:226–9.Google Scholar

  • 15.

    Gadisseur R, Chapelle JP, Cavalier E. A new tool in the field of in-vitro diagnosis of allergy: preliminary results in the comparison of ImmunoCAP(c) 250 with the ImmunoCAP(c) ISAC. Clin Chem Lab Med 2011;49:277–80.Google Scholar

  • 16.

    Fonseca P, Tavares-Ratado P, Tomaz CT. Interference of Dermatophagoides’ specific immunoglobulins G in the quantification of mite’s specific immunoglobulins E. J Immunoassay Immunochem 2009;30:338–47.Google Scholar

About the article

Corresponding author: Janneke Ruinemans-Koerts, PhD, Department of Clinical Chemistry and Haematology, Rijnstate Hospital, Wagnerlaan 55, 6815 AD Arnhem, The Netherlands, Phone: +31 (0)88-0058888


Received: 2016-03-03

Accepted: 2016-06-24

Published Online: 2016-07-30

Published in Print: 2017-02-01


Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

Research funding: None declared.

Employment or leadership: None declared.

Honorarium: None declared.

Competing interests: The funding organization(s) played no role in the study design; in the collection, analysis, and interpretation of data; in the writing of the report; or in the decision to submit the report for publication.


Citation Information: Clinical Chemistry and Laboratory Medicine (CCLM), Volume 55, Issue 2, Pages 248–253, ISSN (Online) 1437-4331, ISSN (Print) 1434-6621, DOI: https://doi.org/10.1515/cclm-2016-0172.

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