ArticleMolecular immunology2013
Structural and bioinformatic analysis of the kiwifruit allergen Act d 11, a member of the family of ripening-related proteins.
Article in Molecular immunology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 56 citations in OpenAlex.
- Identification of potential molecular markers for detection of lengthy chilled storage ofHeliyon · 2024Article
- Identification of a 17 kDa protein that is a potentially novel antigen of lettuce-associated respiratory allergy in farmers.Immunity, inflammation and disease · 2023Article
- Structural Basis of the Immunological Cross-Reactivity between Kiwi and Birch Pollen.Foods (Basel, Switzerland) · 2023Article
- Genome-Wide Evolutionary Characterization and Expression Analysis of Major Latex Protein (MLP) Family Genes in Tomato.International journal of molecular sciences · 2023Article
- Role of Small Molecule Ligands in IgE-Mediated Allergy.Current allergy and asthma reports · 2023Review
- Genome-wide characterization of major latex protein gene family in peanut and expression analyses under drought and waterlogging stress.Frontiers in plant science · 2023Article
- Functional Studies of Plant Latex as a Rich Source of Bioactive Compounds: Focus on Proteins and Alkaloids.International journal of molecular sciences · 2021Review
- Combined Protein and Alkaloid Research ofInternational journal of molecular sciences · 2021Article
- Allergens and their associated small molecule ligands-their dual role in sensitization.Allergy · 2021Review
- Proteome changes in pepper (Capsicum annuum L.) leaves induced by the green peach aphid (Myzus persicae Sulzer).BMC plant biology · 2021Article
- Structural Characterization of Act c 10.0101 and Pun g 1.0101-Allergens from the Non-Specific Lipid Transfer Protein Family.Molecules (Basel, Switzerland) · 2021Article
- The Nicotiana tabacum L. major latex protein-like protein 423 (NtMLP423) positively regulates drought tolerance by ABA-dependent pathway.BMC plant biology · 2020Article
- Molecular approach to a patient's tailored diagnosis of the oral allergy syndrome.Clinical and translational allergy · 2020Review
- Plant-Made Bet v 1 for Molecular Diagnosis.Frontiers in plant science · 2019Article
- Genome-wide evolutionary characterization and expression analyses of major latex protein (MLP) family genes in Vitis vinifera.Molecular genetics and genomics : MGG · 2018Article
- Integrated Phloem Sap mRNA and Protein Expression Analysis Reveals Phytoplasma-infection Responses in Mulberry.Molecular & cellular proteomics : MCP · 2018Article
- Current (Food) Allergenic Risk Assessment: Is It Fit for Novel Foods? Status Quo and Identification of Gaps.Molecular nutrition & food research · 2018Review
- Article
- Recombinant Allergens in Structural Biology, Diagnosis, and Immunotherapy.International archives of allergy and immunology · 2017Review
- Diagnosing allergic sensitizations in the third millennium: why clinicians should know allergen molecule structures.Clinical and translational allergy · 2017Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 4 countries.
Funding
Abstract
The allergen Act d 11, also known as kirola, is a 17 kDa protein expressed in large amounts in ripe green and yellow-fleshed kiwifruit. Ten percent of all kiwifruit-allergic individuals produce IgE specific for the protein. Using X-ray crystallography, we determined the first three-dimensional structures of Act d 11, produced from both recombinant expression in Escherichia coli and from the natural source (kiwifruit). While Act d 11 is immunologically correlated with the birch pollen allergen Bet v 1 and other members of the pathogenesis-related protein family 10 (PR-10), it has low sequence similarity to PR-10 proteins. By sequence Act d 11 appears instead to belong to the major latex/ripening-related (MLP/RRP) family, but analysis of the crystal structures shows that Act d 11 has a fold very similar to that of Bet v 1 and other PR-10 related allergens regardless of the low sequence identity. The structures of both the natural and recombinant protein include an unidentified ligand, which is relatively small (about 250 Da by mass spectrometry experiments) and most likely contains an aromatic ring. The ligand-binding cavity in Act d 11 is also significantly smaller than those in PR-10 proteins. The binding of the ligand, which we were not able to unambiguously identify, results in conformational changes in the protein that may have physiological and immunological implications. Interestingly, the residue corresponding to Glu45 in Bet v 1 (Glu46), which is important for IgE binding to the birch pollen allergen, is conserved in Act d 11, even though it is not in other allergens with significantly higher sequence identity to Bet v 1. We suggest that the so-called Gly-rich loop (or P-loop), which is conserved in all PR-10 allergens, may be responsible for IgE cross-reactivity between Bet v 1 and Act d 11.
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