Structural characteristics of lipocalin allergens: Crystal structure of the immunogenic dog allergen Can f 6

English version

Autoři: Gina M. Clayton ^aff001; Janice White ^aff001; Schuyler Lee ^aff001; John W. Kappler ^aff001; Sanny K. Chan ^aff001
Působiště autorů: Department of Biomedical Research, National Jewish Health, Denver, Colorado, United States of America ^aff001; Program in Structural Biology and Biochemistry, University of Colorado Denver School of Medicine, Aurora, Colorado, United States of America ^aff002; Department of Biochemistry and Molecular Genetics, University of Colorado Denver School of Medicine, Aurora, Colorado, United States of America ^aff003; Department of Immunology and Microbiology, University of Colorado Denver School of Medicine, Aurora, Colorado, United States of America ^aff004; Department of Pediatrics, University of Colorado Denver School of Medicine, Aurora, Colorado, United States of America ^aff005; Division of Pediatric Allergy-Immunology, National Jewish Health, Denver, Colorado, United States of America ^aff006
Vyšlo v časopise: PLoS ONE 14(9)
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pone.0213052

Souhrn

Lipocalins represent the most important protein family of the mammalian respiratory allergens. Four of the seven named dog allergens are lipocalins: Can f 1, Can f 2, Can f 4, and Can f 6. We present the structure of Can f 6 along with data on the biophysical and biological activity of this protein in comparison with other animal lipocalins. The Can f 6 structure displays the classic lipocalin calyx-shaped ligand binding cavity within a central β-barrel similar to other lipocalins. Despite low sequence identity between the different dog lipocalin proteins, there is a high degree of structural similarity. On the other hand, Can f 6 has a similar primary sequence to cat, horse, mouse lipocalins as well as a structure that may underlie their cross reactivity. Interestingly, the entrance to the ligand binding pocket is capped by a His instead of the usually seen Tyr that may help select its natural ligand binding partner. Our highly pure recombinant Can f 6 is able to bind to human IgE (hIgE) demonstrating biological antigenicity.

Klíčová slova:

Biology and life sciences – Biochemistry – Organisms – Eukaryota – Physical sciences – Research and analysis methods – Proteins – Molecular biology – Macromolecular structure analysis – Animals – Medicine and health sciences – Vertebrates – Amniotes – Mammals – Dogs – Clinical medicine – Clinical immunology – Immunology – Physics – Condensed matter physics – Solid state physics – Crystallography – Crystal structure – Allergies – Cats – Glycobiology – Post-translational modification – Protein structure – Phosphorylation – Glycosylation – Allergens – Protein structure comparison – Crystallographic techniques – Crystal structure refinement

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Structural characteristics of lipocalin allergens: Crystal structure of the immunogenic dog allergen Can f 6

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