7DRU

Crystal Structure of the Dog Lipocalin Allergen Can f 1

7DRU の概要

• エントリーDOI: 10.2210/pdb7dru/pdb
• 分子名称: Major allergen Can f 1 (2 entities in total)
• 機能のキーワード: lipocalin allergen, allergen
• 由来する生物種: Canis lupus familiaris (Dog)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 125119.23

構造登録者

Suda, K.,Muroya, H.,Nishimura, S.,Inui, T. (登録日: 2020-12-29, 公開日: 2021-11-10, 最終更新日: 2024-11-13)

主引用文献

Nakatsuji, M.,Sugiura, K.,Suda, K.,Sakurai, M.,Ubatani, M.,Muroya, H.,Okubo, R.,Noguchi, R.,Kamata, Y.,Fukutomi, Y.,Ishibashi, O.,Nishimura, S.,Inui, T.
Structure-based prediction of the IgE epitopes of the major dog allergen Can f 1.
Febs J., 289:1668-1679, 2022

PubMed Abstract: Allergy to dogs has become increasingly prominent worldwide. Seven dog allergens have been identified, including Canis familiaris allergen 1-7 (Can f 1-7). Although Can f 1 is a major dog allergen sensitized to 50-75% of dog-allergic subjects, its IgE epitopes have not been identified. The structural analysis of an allergen is important to identify conformational epitopes. In this study, we generated a recombinant Can f 1 protein and determined its crystal structure using X-ray crystallography. Can f 1 had a typical lipocalin fold, which is composed of an eight-stranded β-barrel and α-helix, and has high similarity to Can f 2, Can f 4, and Can f 6 in overall structure. However, the localizations of surface charges on these proteins were quite different. Based on sequence alignment and tertiary structure, we predicted five critical residues (His86, Glu98, Arg111, Glu138, and Arg152) for the IgE epitopes. The relevance of these residues to IgE reactivity was assessed by generating Can f 1 mutants with these residues substituted for alanine. Although the effects of the mutation on IgE binding depended on the sera of dog-allergic patients, H86A and R152A mutants showed reduced IgE reactivity compared with wild-type Can f 1. These results suggest that Can f 1 residues His86 and Arg152 are candidates for the IgE conformational epitope.

PubMed: 34699686
DOI: 10.1111/febs.16252

実験手法

X-RAY DIFFRACTION (2.5 Å)