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Allergy1993; 48(7); 535-541; doi: 10.1111/j.1398-9995.1993.tb01111.x

Comparison of IgE-binding antigens in horse dander and a mixture of horse hair and skin scrapings.

Abstract: Extracts of horse dander (HD) and horse hair and skin scrapings (HHSS) have been compared with respect to their content of proteins and carbohydrates. The protein content of HD is more than double that of HHSS, while the carbohydrate content is of the same order. SDS-PAGE and IEF, both combined with immunoblotting, and CIE/CRIE showed the IgE-binding ability of the proteins/glycoproteins present in the two extracts. SDS-PAGE/immunoblotting showed the presence of mainly the same IgE-binding bands in the two extracts. Nine were detected in HD, and seven in HHSS. Four of these were glycoproteins. The most important allergen was a glycoprotein with molecular mass of 27 kDa showing IgE-binding ability to the 16 patient sera available. Another important allergen with molecular mass of 67 kDa is probably horse albumin. IEF/immunoblotting showed the presence of a glycoprotein with IgE-binding ability at pH 3.2 in both extracts. Tandem CRIE showed that both extracts contained the same four allergens as major allergens. In addition, as we observed when analyzing both extracts in CRIE against 16 different patient sera, each extract contained allergens not present in the other extract. We may conclude from this investigation that commercial allergen extracts to be used in diagnosis and immunotherapy should include both horse dander and horse hair and skin scrapings in the starting material for the preparation of extracts. If not, allergens which may be of importance for some patients will be missing.
Publication Date: 1993-10-01 PubMed ID: 8238811DOI: 10.1111/j.1398-9995.1993.tb01111.xGoogle Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The research article seeks to compare the content and functionality of proteins and carbohydrates in extracts from horse dander (HD) and horse hair and skin scrapings (HHSS) to understand their roles in allergies.

Overview of the Study

  • The study aimed at comparing the protein and carbohydrate content of horse dander (HD) and extracts of horse hair and skin scrapings (HHSS). This comparison was critical in understanding the properties of allergenic entities in these sources. Allergic reactions are often caused by proteins and glycoproteins and understanding the content of these substances can help determine the most potent sources of allergens.

Methods and Observations

  • Research methods such as sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing (IEF) along with immunoblotting were employed to examine the proteins and glycoproteins in the extracts.
  • The protein content in HD was more than double that of HHSS. However, the carbohydrate contents were relatively the same.
  • Nine IgE-binding bands were detected in HD and seven in HHSS, showing how many different types of allergens may be present in each extract. Of the total IgE-binding bands, four were glycoproteins which are often more potent allergens.
  • The study identified a glycoprotein with a molecular weight of 27kDa as the most important allergen. It could bind to IgE in all 16 patient sera tested.
  • Another significant allergen identified had a molecular weight of 67kDa. This allergen is likely horse albumin.

Key Findings and Recommendations

  • The study found a glycoprotein with IgE-binding ability in both extracts at pH 3.2.
  • The extracts contained the same four major allergens, but each also had unique allergens not present in the other. This understanding implies that a patient could be allergic to one extract and not the other.
  • The findings lead to conclusion that commercial allergen extracts should include both horse dander and horse hair and skin scrapings for preparing extracts. The purpose such move is to ensure no important allergens are left out, which can be particularly critical for some patients.

Cite This Article

APA
Fjeldsgaard BE, Paulsen BS. (1993). Comparison of IgE-binding antigens in horse dander and a mixture of horse hair and skin scrapings. Allergy, 48(7), 535-541. https://doi.org/10.1111/j.1398-9995.1993.tb01111.x

Publication

ISSN: 0105-4538
NlmUniqueID: 7804028
Country: Denmark
Language: English
Volume: 48
Issue: 7
Pages: 535-541

Researcher Affiliations

Fjeldsgaard, B E
  • Department of Pharmacognosy, Institute of Pharmacy, Oslo, Norway.
Paulsen, B S

    MeSH Terms

    • Adolescent
    • Adult
    • Aged
    • Allergens / chemistry
    • Allergens / immunology
    • Animals
    • Antigen-Antibody Reactions
    • Antigens / analysis
    • Antigens / immunology
    • Carbohydrates / analysis
    • Electrophoresis, Polyacrylamide Gel
    • Female
    • Hair / immunology
    • Horses / immunology
    • Humans
    • Hypersensitivity / immunology
    • Immunoblotting
    • Immunoelectrophoresis, Two-Dimensional
    • Immunoglobulin E / immunology
    • Isoelectric Focusing
    • Male
    • Middle Aged
    • Proteins / analysis
    • Skin / immunology

    Citations

    This article has been cited 6 times.
    1. Victor S, Lampa E, Rask Andersen A, Gafvelin G, Grönlund H, Elfman L. Measurement of Horse Allergens Equ c 1 and Equ c 2: A Comparison among Breeds.. Int Arch Allergy Immunol 2022;183(11):1166-1177.
      doi: 10.1159/000525960pubmed: 36049466google scholar: lookup
    2. Maryniak NZ, Sancho AI, Hansen EB, Bøgh KL. Alternatives to Cow's Milk-Based Infant Formulas in the Prevention and Management of Cow's Milk Allergy.. Foods 2022 Mar 23;11(7).
      doi: 10.3390/foods11070926pubmed: 35407012google scholar: lookup
    3. Victor S, Binnmyr J, Lampa E, Rask-Andersen A, Elfman L. Levels of horse allergen Equ c 4 in dander and saliva from ten horse breeds.. Clin Exp Allergy 2019 May;49(5):701-711.
      doi: 10.1111/cea.13362pubmed: 30716182google scholar: lookup
    4. Majorek KA, Porebski PJ, Dayal A, Zimmerman MD, Jablonska K, Stewart AJ, Chruszcz M, Minor W. Structural and immunologic characterization of bovine, horse, and rabbit serum albumins.. Mol Immunol 2012 Oct;52(3-4):174-82.
      doi: 10.1016/j.molimm.2012.05.011pubmed: 22677715google scholar: lookup
    5. Grier TJ. Laboratory methods for allergen extract analysis and quality control.. Clin Rev Allergy Immunol 2001 Oct;21(2-3):111-40.
      doi: 10.1385/CRIAI:21:2-3:111pubmed: 11725601google scholar: lookup
    6. Goubran Botros H, Gregoire C, Rabillon J, David B, Dandeu JP. Cross-antigenicity of horse serum albumin with dog and cat albumins: study of three short peptides with significant inhibitory activity towards specific human IgE and IgG antibodies.. Immunology 1996 Jul;88(3):340-7.