Characterization of a Major Allergen from Mongolian Oak, Quercus mongolica, a Dominant Species of Oak in Korea

• Published in: International archives of allergy and immunology Vol. 174; no. 2; p. 77
• Main Authors: Lee, June Yong, Yang, Misuk, Jeong, Kyoung Yong, Sim, Da Woon, Park, Jin Hee, Park, Kyung Hee, Lee, Jae-Hyun, Park, Jung-Won
• Format: Journal Article
• Language: English
• Published: Switzerland 01.11.2017
• Subjects: Adolescent; Adult; Aged; Amino Acid Sequence; Antigens, Plant - chemistry; Antigens, Plant - genetics; Antigens, Plant - immunology; Base Sequence; Basophils - immunology; Child; Cloning, Molecular; Female; Humans; Immunoglobulin E - blood; Immunoglobulin E - immunology; Male; Middle Aged; Plant Proteins - immunology; Pollen - immunology; Protein Structure, Secondary; Quercus - chemistry; Quercus - immunology; Republic of Korea; Rhinitis, Allergic, Seasonal - diagnosis; Rhinitis, Allergic, Seasonal - immunology; Trees - immunology; Young Adult; Oak; Allergens; Pathogenesis-related protein 10; Pollinosis
• DOI: 10.1159/000481092

Oaks are the most common trees in Korean forests, and Mongolian oak, Quercus mongolica, is the dominant species. However, no allergen has been characterized from Mongolian oak. In this study, we tried to characterize a major allergen from Mongolian oak. A molecule homologous to pathogenesis-related 10 (PR-10)-like protein, Que m 1, was cloned by RT-PCR. Its recombinant protein, along with Que a 1, an allergen from white oak (Q. alba), was produced. The allergenicity and diagnostic value of recombinant Que m 1, Que a 1, and Bet v 1 proteins were compared by ELISA using sera from oak-sensitized subjects. A basophil activation test was also performed using CD63 expression as an activation marker. Que m 1 sequence shares 57.5-96.2% amino acid sequence identity with PR-10-like allergens from various plants. Specific IgE to recombinant Que m 1, Que a 1, and Bet v 1 were detected in 92.0, 74.0, and 38.0% of 50 serum samples from Korean tree pollinosis patients. Recombinant Que m 1 was able to inhibit IgE reactivity to Que a 1 and Bet v 1, indicating its strong cross-reactivity. The activation patterns of basophils from 5 patients were similar in terms of the CD63 expression and protein concentration of challenged Bet v 1 and Que m 1. A major allergen, Que m 1, was cloned, and its recombinant protein was produced from Mongolian oak, a dominant species in Korea. Recombinant Que m 1 is potentially useful for the diagnosis and treatment of tree pollinosis in Korea.