Lipocalins as allergens

被引:53
作者
Mäntyjärvi, R [1 ]
Rautiainen, J [1 ]
Virtanen, T [1 ]
机构
[1] Univ Kuopio, Dept Clin Microbiol, FIN-70211 Kuopio, Finland
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2000年 / 1482卷 / 1-2期
关键词
allergen; lipocalin; epitope; animal allergy;
D O I
10.1016/S0167-4838(00)00139-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The term allergy refers to clinical conditions caused by an inappropriate immune response to innocuous proteins in genetically predisposed persons. Allergens of animal origin are responsible for a significant proportion of allergies. In recent years, it has become evident that practically all respiratory animal allergens characterized at the molecular level belong to the lipocalin family of proteins. The current list comprises the major allergens of horse, cow, dog, mouse, rat and cockroach as well as beta -lactoglobulin of cow's milk. While the molecular structure of all these allergens is known, far less information is available regarding their immunological characteristics. Knowing the way the immune system recognizes these allergens and reacts to them might, however, be the key for discovering the common denominator of the allergenicity of lipocalins. The human body contains numerous endogenous lipocalins, and the immune system has to adapt to their presence. We have proposed that under these conditions the immune response against the lipocalin allergens which are structurally related to endogenous lipocalins might be the pathway to allergy in genetically predisposed persons. The same might well apply also to other allergens with homologous endogenous counterparts. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:308 / 317
页数:10
相关论文
共 95 条
[1]   Immunology of human helminth infection [J].
Allen, JE ;
Maizels, RM .
INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY, 1996, 109 (01) :3-10
[2]  
AOYAMA K, 1992, BRIT J IND MED, V49, P41
[3]   Cloning of cockroach allergen, Bla g 4, identifies ligand binding proteins (or calycins) as a cause of IgE antibody responses [J].
Arruda, LK ;
Vailes, LD ;
Hayden, ML ;
Benjamin, DC ;
Chapman, MD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (52) :31196-31201
[4]  
Ausubel LJ, 1997, J IMMUNOL, V159, P2502
[5]   A MAJOR CONTINUOUS ALLERGENIC EPITOPE OF BOVINE BETA-LACTOGLOBULIN RECOGNIZED BY HUMAN IGE BINDING [J].
BALL, G ;
SHELTON, MJ ;
WALSH, BJ ;
HILL, DJ ;
HOSKING, CS ;
HOWDEN, MEH .
CLINICAL AND EXPERIMENTAL ALLERGY, 1994, 24 (08) :758-764
[6]   ALLERGEN SKIN-TEST REACTIVITY IN A COMMUNITY POPULATION-SAMPLE - CORRELATION WITH AGE, HISTAMINE SKIN REACTIONS, AND TOTAL SERUM IMMUNOGLOBULIN-E [J].
BARBEE, RA ;
BROWN, WG ;
KALTENBORN, W ;
HALONEN, M .
JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY, 1981, 68 (01) :15-19
[7]   In vivo antagonism of a T cell response by an endogenously expressed ligand [J].
Basu, D ;
Williams, CB ;
Allen, PM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (24) :14332-14336
[8]   Purification and identification of allergenic alpha(2u)-globulin species of rat urine [J].
Bayard, C ;
Holmquist, L ;
Vesterberg, O .
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1996, 1290 (02) :129-134
[9]   CHARACTERIZATION OF EXTRACT OF DOG HAIR AND DANDRUFF FROM 6 DIFFERENT DOG BREEDS BY QUANTITATIVE IMMUNOELECTROPHORESIS - IDENTIFICATION OF ALLERGENS BY CROSSED RADIO-IMMUNOELECTROPHORESIS (CRIE) [J].
BLANDS, J ;
LOWENSTEIN, H ;
WEEKE, B .
ACTA ALLERGOLOGICA, 1977, 32 (03) :147-&
[10]   Separation of horse dander allergen proteins by two-dimensional electrophoresis - Molecular characterisation and identification of Equ c 2.0101 and Equ c 2.0102 as lipocalin proteins [J].
Bulone, V ;
Krogstad-Johnsen, T ;
Smestad-Paulsen, B .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1998, 253 (01) :202-211