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European journal of biochemistry2001; 268(10); 3126-3136; doi: 10.1046/j.1432-1327.2001.02217.x

Biochemical characterization and surfactant properties of horse allergens.

Abstract: A new allergen from horse dander, Equ c 5 has been purified. Its biochemical and biophysical properties have been characterized and compared with those of Equ c 1, Equ c 2 and Equ c 4. Their molecular masses, determined by mass spectrometry, were 22 kDa for Equ c 1, 16 kDa for Equ c 2, 18.7 kDa for Equ c 4 and 16.7 kDa for Equ c 5. Their pI values were between 3.8 and 5.25. Equ c 2 and Equ c 5 are not glycosylated, while Equ c 4 contains a tri-antennary tri-sialylated N-linked glycan. Linkages of terminal N-acetylneuraminic acid to galactose were: alpha-(2-->6) in Equ c 4, and both alpha-(2-->3) and alpha-(2-->6) in Equ c 1. Oligosaccharide portions of Equ c 1 or Equ c 4 were barely involved in IgE-immunoreactivity. Partial N-terminal sequence of Equ c 4 shares a significant sequence homology with the rat submandibular gland protein A. No matching was found for two internal peptides of Equ c 5. Surfactant properties of horse allergens as well as other proteins were investigated. In contrast to Equ c 2 and Equ c 3, solutions of Equ c 1, Equ c 4 and Equ c 5 significantly lowered the surface tension. Relationship between a property such as this, involving oriented hydrophobic patches of a molecule and allergenicity, is addressed.
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Publication Date: 2001-05-19 PubMed ID: 11358533DOI: 10.1046/j.1432-1327.2001.02217.xGoogle Scholar: Lookup
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Summary

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The article details the purification and characterization of a newly discovered allergen found in horse dander, known as Equ c 5. The allergen’s properties were compared to those of similar allergens, Equ c 1, Equ c 2 and Equ c 4. The study also investigates the surfactant properties and allergenicity of the proteins.

Characterization of Allergens

  • The allergens Equ c 1, Equ c 2, Equ c 4 and Equ c 5 were studied for their biochemical and biophysical properties.
  • Their molecular masses, determined by mass spectrometry were: 22 kDa for Equ c 1, 16 kDa for Equ c 2, 18.7 kDa for Equ c 4 and 16.7 kDa for Equ c 5.
  • The pI values of the allergens, which are measures of acidity, were found to be between 3.8 and 5.25, suggesting they are mildly acidic proteins.

Glycosylation of Allergens

  • Glycosylation, the process of adding carbohydrate groups to a protein, was investigated in all allergens. Equ c 2 and Equ c 5 were found to be not glycosylated, while Equ c 4 was found to have a tri-antennary tri-sialylated N-linked glycan, a specific structure of carbohydrate.
  • The linkages of terminal N-acetylneuraminic acid to galactose, a type of sugar connection in the carbohydrate group, varied among allergens.
  • The oligosaccharide portions of Equ c 1 or Equ c 4 were noted to have little role in IgE-immunoreactivity, which is related to the allergic reaction in the body.

Protein Sequence Homology and Surfactant Properties

  • A partial N-terminal sequence of Equ c 4 was found to have significant sequence homology with the rat submandibular gland protein A, suggesting similarities between the horse allergen and this rat protein.
  • Surfactant properties of the horse allergens were investigated. Surfactants lower the surface tension of a liquid. Equ c 1, Equ c 4 and Equ c 5 were found to significantly lower surface tension when in solution, unlike Equ c 2 and Equ c 3.
  • The relationship between surfaces’ hydrophobicity and the allergenicity is also addressed in the study.

Cite This Article

APA
Goubran Botros H, Poncet P, Rabillon J, Fontaine T, Laval JM, David B. (2001). Biochemical characterization and surfactant properties of horse allergens. Eur J Biochem, 268(10), 3126-3136. https://doi.org/10.1046/j.1432-1327.2001.02217.x

Publication

European journal of biochemistry
ISSN: 0014-2956
NlmUniqueID: 0107600
Country: England
Language: English
Volume: 268
Issue: 10
Pages: 3126-3136

Researcher Affiliations

Goubran Botros, H
  • Unité d'Immuno-Allergie, Institut Pasteur, Paris France. hgbotros@pasteur.fr
Poncet, P
    Rabillon, J
      Fontaine, T
        Laval, J M
          David, B

            MeSH Terms

            • Allergens / chemistry
            • Allergens / metabolism
            • Amino Acid Sequence
            • Animals
            • Blotting, Western
            • Dose-Response Relationship, Drug
            • Electrophoresis, Polyacrylamide Gel
            • Enzyme-Linked Immunosorbent Assay
            • Glycoproteins / chemistry
            • Glycoproteins / metabolism
            • Glycosylation
            • Horses
            • Humans
            • Hydrogen-Ion Concentration
            • Immunoglobulin E / metabolism
            • Isoelectric Focusing
            • Kinetics
            • Mass Spectrometry
            • Molecular Sequence Data
            • Monosaccharides / chemistry
            • Oligosaccharides / chemistry
            • Protein Binding
            • Rats
            • Sequence Analysis, Protein
            • Sequence Homology, Amino Acid
            • Surface-Active Agents / chemistry
            • Time Factors

            Citations

            This article has been cited 16 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. Popescu FD, Ganea CS, Panaitescu C, Vieru M. Molecular diagnosis in cat allergy. World J Methodol 2021 May 20;11(3):46-60.
              doi: 10.5662/wjm.v11.i3.46pubmed: 34026578google scholar: lookup
            3. Haka J, Niemi MH, Mattila P, Jänis J, Takkinen K, Rouvinen J. Development of hypoallergenic variants of the major horse allergen Equ c 1 for immunotherapy by rational structure based engineering. Sci Rep 2019 Dec 27;9(1):20148.
              doi: 10.1038/s41598-019-56812-1pubmed: 31882906google scholar: lookup
            4. 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
            5. Zahradnik E, Janssen-Weets B, Sander I, Kendzia B, Mitlehner W, May C, Raulf M. Lower allergen levels in hypoallergenic Curly Horses? A comparison among breeds by measurements of horse allergens in hair and air samples. PLoS One 2018;13(12):e0207871.
              doi: 10.1371/journal.pone.0207871pubmed: 30540798google scholar: lookup
            6. Zahradnik E, Raulf M. Respiratory Allergens from Furred Mammals: Environmental and Occupational Exposure. Vet Sci 2017 Aug 4;4(3).
              doi: 10.3390/vetsci4030038pubmed: 29056697google scholar: lookup
            7. Hilger C, van Hage M, Kuehn A. Diagnosis of Allergy to Mammals and Fish: Cross-Reactive vs. Specific Markers. Curr Allergy Asthma Rep 2017 Aug 22;17(9):64.
              doi: 10.1007/s11882-017-0732-zpubmed: 28831729google scholar: lookup
            8. Zahradnik E, Raulf M. Animal allergens and their presence in the environment. Front Immunol 2014;5:76.
              doi: 10.3389/fimmu.2014.00076pubmed: 24624129google scholar: lookup
            9. Vance SJ, McDonald RE, Cooper A, Smith BO, Kennedy MW. The structure of latherin, a surfactant allergen protein from horse sweat and saliva. J R Soc Interface 2013 Aug 6;10(85):20130453.
              doi: 10.1098/rsif.2013.0453pubmed: 23782536google scholar: lookup
            10. Gawlik R, Pitsch T, Dubuske L. Anaphylaxis as a manifestation of horse allergy. World Allergy Organ J 2009 Aug;2(8):185-9.
              doi: 10.1097/WOX.0b013e3181b2fe51pubmed: 23283110google scholar: lookup
            11. Hilger C, Kuehn A, Hentges F. Animal lipocalin allergens. Curr Allergy Asthma Rep 2012 Oct;12(5):438-47.
              doi: 10.1007/s11882-012-0283-2pubmed: 22791068google scholar: lookup
            12. Liccardi G, Emenius G, Merritt AS, Salzillo A, D'Amato M, D'Amato G. Direct and indirect exposure to horse: risk for sensitization and asthma. Curr Allergy Asthma Rep 2012 Oct;12(5):429-37.
              doi: 10.1007/s11882-012-0280-5pubmed: 22717671google scholar: lookup
            13. Bartlett JA, Gakhar L, Penterman J, Singh PK, Mallampalli RK, Porter E, McCray PB Jr. PLUNC: a multifunctional surfactant of the airways. Biochem Soc Trans 2011 Aug;39(4):1012-6.
              doi: 10.1042/BST0391012pubmed: 21787339google scholar: lookup
            14. Gakhar L, Bartlett JA, Penterman J, Mizrachi D, Singh PK, Mallampalli RK, Ramaswamy S, McCray PB Jr. PLUNC is a novel airway surfactant protein with anti-biofilm activity. PLoS One 2010 Feb 9;5(2):e9098.
              doi: 10.1371/journal.pone.0009098pubmed: 20161732google scholar: lookup
            15. McDonald RE, Fleming RI, Beeley JG, Bovell DL, Lu JR, Zhao X, Cooper A, Kennedy MW. Latherin: a surfactant protein of horse sweat and saliva. PLoS One 2009 May 29;4(5):e5726.
              doi: 10.1371/journal.pone.0005726pubmed: 19478940google scholar: lookup
            16. Trifonova D, Curin M, Riabova K, Karsonova A, Keller W, Grönlund H, Käck U, Konradsen JR, van Hage M, Karaulov A, Valenta R. Allergenic Activity of Individual Cat Allergen Molecules. Int J Mol Sci 2023 Nov 24;24(23).
              doi: 10.3390/ijms242316729pubmed: 38069052google scholar: lookup
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