Molecular characterization of timothy grass pollen group V allergens

International Archives of Allergy and Immunology
W M BeckerM Schlaak

Abstract

Phl p V is the dominant allergen of timothy grass (Phleum pratense) with two isoforms having the apparent molecular weights of 38 (Phl p Va) and 32 kD (Phl p Vb) under Western blot conditions. Two-dimensional electrophoresis/immunoblotting reveals that each isoform is split into at least four isoallergens. Structural differences in the isoforms are shown by N-terminal sequencing (only 60% identity), by reaction patterns of monoclonal antibodies and, more convincingly, by enzymic degradation of purified isoforms followed by immunologic fingerprinting. These findings are confirmed by the deduced primary protein structure of cloned Phl p Va and Phl p Vb. Experiments with IgE--affinity-purified by immobilized recombinant allergens or their fragments--reveal identical epitopes and at least one different epitope between the isoforms. Furthermore, on Phl p Va we can localize different IgE-reactive epitopes at the C terminus as well as the N terminus. By probing serum from 11 patients on recombinant C- or N-terminal fragments, an individual reaction pattern was found. Testing the histamine liberation potency of the fragments, we found the N-terminal fragment of Phl p Va to be superior to that of the C-terminal fragment or the whole mol...Continue Reading

Citations

Feb 21, 2008·Wiener medizinische Wochenschrift·Brigitte Hantusch, Erika Jensen-Jarolim
Jan 1, 1987·Neuropsychologia·J Smith
Jul 9, 2002·Clinical and Experimental Allergy : Journal of the British Society for Allergy and Clinical Immunology·Ronald van Ree
Dec 4, 2004·The Journal of Allergy and Clinical Immunology·Brigitte HantuschErika Jensen-Jarolim
Apr 25, 2012·Allergology International : Official Journal of the Japanese Society of Allergology·Alena SekerkovaIlja Striz
Jan 1, 1997·Clinical Reviews in Allergy & Immunology·D A Vuitton
Jun 8, 2021·Molecular Immunology·Nicolas VisezPascal Poncet

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