Molecular cloning, expression and immunological characterisation of Lol p 5C, a novel allergen isoform of rye grass pollen demonstrating high IgE reactivity

• Published in: FEBS letters 1999-12, Vol.462 (3), p.435-441
• Main Authors: Suphioglu, Cenk, Mawdsley, David, Schäppi, George, Gruehn, Sabine, de Leon, Maria, Rolland, Jennifer M., O’Hehir, Robyn E.
• Format: Article
• Language: English
• Subjects: Allergens; Amino Acid Sequence; Antibodies, Monoclonal - metabolism; Antigens, Plant; Base Sequence; cDNA cloning; Cloning, Molecular; DNA, Complementary - metabolism; Electrophoresis, Gel, Two-Dimensional; Gene Library; Human IgE; Humans; Hypersensitivity - immunology; Immunoblotting; Immunoglobulin E - metabolism; Isoform; Lol p 5C; Lolium - genetics; Lolium perenne; Molecular Sequence Data; Plant Proteins - biosynthesis; Plant Proteins - genetics; Plant Proteins - immunology; Pollen allergen; Protein Isoforms - biosynthesis; Protein Isoforms - genetics; Protein Isoforms - immunology; Sequence Homology, Amino Acid; Time Factors
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(99)01576-8

A novel isoform of a major rye grass pollen allergen Lol p 5 was isolated from a cDNA expression library. The new isoform, Lol p 5C, shares 95% amino acid sequence identity with Lol p 5A. Both isoforms demonstrated shared antigenic activity but different allergenic activities. Recombinant Lol p 5C demonstrated 100% IgE reactivity in 22 rye grass pollen sensitive patients. In comparison, recombinant Lol p 5A showed IgE reactivity in less than 64% of the patients. Therefore, Lol p 5C represents a novel and highly IgE-reactive isoform allergen of rye grass pollen.