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

Jensen Jarolim, Erika and Pacios, Luis F. and Bianchini, G. and Hofstetter, Gerlinde and Roth Walter, Franziska (2016). Structural similarities of human and mammalian lipocalins, and their function in innate immunity and allergy. "Allergy", v. 71 (n. 3); pp. 286-294. ISSN 0105-4538. https://doi.org/10.1111/all.12797.

Description

Title: Structural similarities of human and mammalian lipocalins, and their function in innate immunity and allergy
Author/s:
  • Jensen Jarolim, Erika
  • Pacios, Luis F.
  • Bianchini, G.
  • Hofstetter, Gerlinde
  • Roth Walter, Franziska
Item Type: Article
Título de Revista/Publicación: Allergy
Date: March 2016
Volume: 71
Subjects:
Freetext Keywords: allergen; animal; canine; iron; lipocalin
Faculty: E.T.S.I. Montes (UPM)
Department: Sistemas y Recursos Naturales
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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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 ?-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.

More information

Item ID: 41250
DC Identifier: http://oa.upm.es/41250/
OAI Identifier: oai:oa.upm.es:41250
DOI: 10.1111/all.12797
Official URL: https://doi.org/10.1111/all.12797
Deposited by: Memoria Investigacion
Deposited on: 29 Aug 2016 10:17
Last Modified: 14 Mar 2019 16:51
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