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Allergy2015; 71(3); 286-294; doi: 10.1111/all.12797

Structural similarities of human and mammalian lipocalins, and their function in innate immunity and allergy.

Abstract: Owners and their domestic animals via skin shedding and secretions, mutually exchange microbiomes, potential pathogens and innate immune molecules. Among the latter especially lipocalins are multifaceted: they may have an immunomodulatory function and, furthermore, they represent one of the most important animal allergen families. The amino acid identities, as well as their structures by superposition modeling were compared among human lipocalins, hLCN1 and hLCN2, and most important animal lipocalin allergens, such as Can f 1, Can f 2 and Can f 4 from dog, Fel d 4 from cats, Bos d 5 from cow's milk, Equ c 1 from horses, and Mus m 1 from mice, all of them representing major allergens. The β-barrel fold with a central molecular pocket is similar among human and animal lipocalins. Thereby, lipocalins are able to transport a variety of biological ligands in their highly conserved calyx-like cavity, among them siderophores with the strongest known capability to complex iron (Fe(3+) ). Levels of human lipocalins are elevated in nonallergic inflammation and cancer, associated with innate immunoregulatory functions that critically depend on ligand load. Accordingly, deficient loading of lipocalin allergens establishes their capacity to induce Th2 hypersensitivity. Our similarity analysis of human and mammalian lipocalins highlights their function in innate immunity and allergy.
Publication Date: 2015-11-23 PubMed ID: 26497994PubMed Central: PMC4949658DOI: 10.1111/all.12797Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Review

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article presents a comparative analysis of human and mammalian lipocalins, focusing on their structure and role in immune response and allergic reactions. The findings of the study highlight the multifunctional nature of lipocalins, their essential role in carrying biological ligands, and how their deficient loading can induce hypersensitivity.

Understanding Lipocalins

  • Lipocalins are proteins that play multiple roles in both humans and animals. They are involved in the immune response system – particularly innate immunity – and are a key component of allergies.
  • These proteins can be exchanged between humans and their domestic animals through skin shedding and secretions, thereby affecting both the human and animal microbiomes.

Comparative Analysis of Human and Animal Lipocalins

  • The research involves a comparison of the amino acid identities and structures of human lipocalins (hLCN1 and hLCN2) and several major animal allergens: Can f 1, Can f 2, and Can f 4 from dogs; Fel d 4 from cats; Bos d 5 from cow’s milk; Equ c 1 from horses; and Mus m 1 from mice.
  • The β-barrel fold, a key structural aspect of lipocalins, displayed similarity across both human and animal proteins. This feature allows the protein to transport a variety of biological ligands.

Role of Lipocalins in Immune Response and Allergies

  • Lipocalins carry diverse biological ligands within their highly conserved, calyx-like cavity. Among these ligands are siderophores, known for their strong affinity with iron (Fe(3+)).
  • In nonallergic inflammation and cancer, human lipocalin levels are found to be elevated. This elevation is associated with innate immune regulatory functions which are heavily dependent on ligand load.
  • When lipocalin allergens are not sufficiently loaded, they can induce a Th2 hypersensitivity – an overactive immune response often associated with allergic reactions.

Conclusions

  • This research emphasizes the importance of lipocalins in the innate immune system and the onset of allergies. The structural similarities between human and mammalian lipocalins suggest potential avenues for studying and treating allergies triggered by animal lipocalin allergens.

Cite This Article

APA
Jensen-Jarolim E, Pacios LF, Bianchini R, Hofstetter G, Roth-Walter F. (2015). Structural similarities of human and mammalian lipocalins, and their function in innate immunity and allergy. Allergy, 71(3), 286-294. https://doi.org/10.1111/all.12797

Publication

ISSN: 1398-9995
NlmUniqueID: 7804028
Country: Denmark
Language: English
Volume: 71
Issue: 3
Pages: 286-294

Researcher Affiliations

Jensen-Jarolim, E
  • The interuniversity Messerli Research Institute, University of Veterinary Medicine Vienna, Medical University Vienna, University Vienna, Vienna, Austria.
  • Institute of Pathophysiology and Allergy Research, Center of Pathophysiology, Infectiology and Immunology, Medical University Vienna, Vienna, Austria.
Pacios, L F
  • Biotechnology Department, Center for Plant Biotechnology and Genomics, ETSI Montes, Technical University of Madrid, Madrid, Spain.
  • Department of Natural Systems and Resources, ETSI Montes, Technical University of Madrid, Madrid, Spain.
Bianchini, R
  • The interuniversity Messerli Research Institute, University of Veterinary Medicine Vienna, Medical University Vienna, University Vienna, Vienna, Austria.
Hofstetter, G
  • The interuniversity Messerli Research Institute, University of Veterinary Medicine Vienna, Medical University Vienna, University Vienna, Vienna, Austria.
Roth-Walter, F
  • The interuniversity Messerli Research Institute, University of Veterinary Medicine Vienna, Medical University Vienna, University Vienna, Vienna, Austria.

MeSH Terms

  • Allergens / chemistry
  • Allergens / immunology
  • Allergens / metabolism
  • Animals
  • Humans
  • Hypersensitivity / immunology
  • Hypersensitivity / metabolism
  • Immune Tolerance
  • Immunity, Innate
  • Immunoglobulin E / immunology
  • Immunomodulation
  • Lipocalins / chemistry
  • Lipocalins / immunology
  • Lipocalins / metabolism
  • Protein Conformation
  • Structure-Activity Relationship
  • Th2 Cells / immunology
  • Th2 Cells / metabolism

Grant Funding

  • F 4606 / Austrian Science Fund FWF

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