ArticleMolecular immunology2014
The major cockroach allergen Bla g 4 binds tyramine and octopamine.
Article in Molecular immunology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Role of Small Molecule Ligands in IgE-Mediated Allergy.Current allergy and asthma reports · 2023Review
- Cockroach allergy: Understanding complex immune responses to develop novel therapies.Molecular immunology · 2023Article
- Structural and ligand binding analysis of the pet allergens Can f 1 and Fel d 7.Frontiers in allergy · 2023Article
- Liposomal Formulations Loaded with a Eugenol Derivative for Application as Insecticides: Encapsulation Studies and In Silico Identification of Protein Targets.Nanomaterials (Basel, Switzerland) · 2022Article
- Mammalian derived lipocalin and secretoglobin respiratory allergens strongly bind ligands with potentially immune modulating properties.Frontiers in allergy · 2022Article
- Allergens and their associated small molecule ligands-their dual role in sensitization.Allergy · 2021Review
- The allergenic activity and clinical impact of individual IgE-antibody binding molecules from indoor allergen sources.The World Allergy Organization journal · 2020Review
- Article
- Current (Food) Allergenic Risk Assessment: Is It Fit for Novel Foods? Status Quo and Identification of Gaps.Molecular nutrition & food research · 2018Review
- New Insights into Cockroach Allergens.Current allergy and asthma reports · 2017Review
- Article
- Interfaces between allergen structure and diagnosis: know your epitopes.Current allergy and asthma reports · 2015Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
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Abstract
Bla g 4 is a male cockroach specific protein and is one of the major allergens produced by Blattella germanica (German cockroach). This protein belongs to the lipocalin family that comprises a set of proteins that characteristically bind small hydrophobic molecules and play a role in a number of processes such as: retinoid and pheromone transport, prostaglandin synthesis and mammalian immune response. Using NMR and isothermal titration calorimetry we demonstrated that Bla g 4 binds tyramine and octopamine in solution. In addition, crystal structure analysis of the complex revealed details of tyramine binding. As tyramine and octopamine play important roles in invertebrates, and are counterparts to vertebrate adrenergic transmitters, we speculate that these molecules are physiological ligands for Bla g 4. The nature of binding these ligands to Bla g 4 sheds light on the possible biological function of the protein. In addition, we performed a large-scale analysis of Bla g 4 and Per a 4 (an allergen from American cockroach) homologs to get insights into the function of these proteins. This analysis together with a structural comparison of Blag 4 and Per a 4 suggests that these proteins may play different roles and most likely bind different ligands. Accession numbers: The atomic coordinates and the structure factors have been deposited to the Protein Data Band under accession codes: 4N7C for native Bla g 4 and 4N7D for the Se-Met Bla g 4 structure.
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