title: 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.
authors.affiliation: Unité d'Immuno-Allergie, Institut Pasteur, Paris France. hgbotros@pasteur.fr
authors.forename: H
authors.initials: H
authors.lastname: Goubran Botros
authors.forename: P
authors.initials: P
authors.lastname: Poncet
authors.forename: J
authors.initials: J
authors.lastname: Rabillon
authors.forename: T
authors.initials: T
authors.lastname: Fontaine
authors.forename: J M
authors.initials: JM
authors.lastname: Laval
authors.forename: B
authors.initials: B
authors.lastname: David
mesh_terms: D000485:Allergens / Q000737:chemistry* / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006023:Glycoproteins / Q000737:chemistry* / Q000378:metabolism*; D006031:Glycosylation; D006736:Horses; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007073:Immunoglobulin E / Q000378:metabolism; D007525:Isoelectric Focusing; D007700:Kinetics; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009005:Monosaccharides / Q000737:chemistry; D009844:Oligosaccharides / Q000737:chemistry; D011485:Protein Binding; D051381:Rats; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid; D013501:Surface-Active Agents / Q000737:chemistry*; D013997:Time Factors
chemical_list: D000485:Allergens; D006023:Glycoproteins; D009005:Monosaccharides; D009844:Oligosaccharides; D013501:Surface-Active Agents; D007073:Immunoglobulin E