Identification of bovine IgG as a major cross-reactive vertebrate meat allergen

被引:50
作者
Ayuso, R
Lehrer, SB
Lopez, M
Reese, G
Ibañez, MD
Esteban, MM
Ownby, DR
Schwartz, H
机构
[1] Tulane Univ, Sch Med, Allergy & Clin Immunol Sect, New Orleans, LA 70112 USA
[2] Hosp Nino Jesus, Madrid, Spain
[3] Hosp Univ La Paz, Madrid, Spain
[4] Henry Ford Hosp, Detroit, MI 48202 USA
[5] Univ Suburban Hlth Ctr, Cleveland, OH USA
关键词
allergens; beef; cross-reactivity; IgG; meat allergy;
D O I
10.1034/j.1398-9995.2000.00285.x
中图分类号
R392 [医学免疫学];
学科分类号
100102 ;
摘要
Background: Although beef is a main source of protein in Western diets, very little has been published on allergic reactions to beef or the main allergens implicated in these reactions. The aim was to evaluate the IgE antibody response to beef in suspected meat-allergic subjects and assess cross-reactivity of beef with other vertebrate meats. Methods: Fifty-seven sera from suspected meat-allergic subjects were tested by grid blot for specific IgE antibodies to vertebrate meats (beef, lamb, pork, venison, and chicken), and the patterns of recognition of meat proteins were assessed by immunoblot studies. Results: A 160-kDa band, identified as bovine IgG, was detected in raw beef in 83% (10/12) of beef-allergic subjects but in only 24% of the beef-tolerant subjects. IgE reactivity to a band of similar mol. mass was detected also in lamb and venison, but rarely in pork or chicken. Complete inhibition of the IgE reactivity to the bovine IgG was obtained with lamb, venison, and milk. IgE reactivity to this band also completely disappeared when beef or lamb extracts were separated under reducing conditions, indicating conformational epitopes. Conclusions: Bovine IgG appears to be a major cross-reacting meal allergen that could predict beef allergy. Further studies with oral IgG challenges should be performed to document the conclusion that in vitro reactivity correlates with clinical hypersensitivity. The role of bovine IgG in other bovine products such as milk, dander, or hair must also be studied, and the hypothesis that it is a crossreacting allergen with other mammalian products validated.
引用
收藏
页码:348 / 354
页数:7
相关论文
共 29 条
[1]   IgE antibody response to vertebrate meat proteins including tropomyosin [J].
Ayuso, R ;
Lehrer, SB ;
Tanaka, L ;
Ibañez, MD ;
Pascual, C ;
Burks, AW ;
Sussman, GL ;
Goldberg, B ;
Lopez, M ;
Reese, G .
ANNALS OF ALLERGY ASTHMA & IMMUNOLOGY, 1999, 83 (05) :399-405
[2]  
BERNHISELBROADBENT J, 1991, PEDIATRICS, V87, P208
[3]   CYANOGEN BROMIDE-ACTIVATED NITROCELLULOSE MEMBRANES - A NEW TOOL FOR IMMUNOPRINT TECHNIQUES [J].
DEMEULEMESTER, C ;
PELTRE, G ;
LAURENT, M ;
PANHELEUX, D ;
DAVID, B .
ELECTROPHORESIS, 1987, 8 (01) :71-73
[4]  
FIOCCHI A, 1995, J AM COLL NUTR, V14, P239
[5]  
FISHER AA, 1977, CUTIS, V19, P561
[6]   IGE BINDING STRUCTURES OF THE MAJOR HOUSE DUST MITE ALLERGEN DER-P-I [J].
GREENE, WK ;
THOMAS, WR .
MOLECULAR IMMUNOLOGY, 1992, 29 (02) :257-262
[7]   IMPROVED SILVER STAINING PROCEDURE FOR FAST STAINING IN PHASTSYSTEM DEVELOPMENT UNIT .1. STAINING OF SODIUM DODECYL-SULFATE GELS [J].
HEUKESHOVEN, J ;
DERNICK, R .
ELECTROPHORESIS, 1988, 9 (01) :28-32
[8]   OCCUPATIONAL CONTACT URTICARIA FROM BEEF ASSOCIATED WITH HAND ECZEMA [J].
JOVANOVIC, M ;
OLIWIECKI, S ;
BECK, MH .
CONTACT DERMATITIS, 1992, 27 (03) :188-189
[9]   ELECTROBLOTTING OF MULTIPLE GELS - A SIMPLE APPARATUS WITHOUT BUFFER TANK FOR RAPID TRANSFER OF PROTEINS FROM POLYACRYLAMIDE TO NITROCELLULOSE [J].
KYHSEANDERSEN, J .
JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS, 1984, 10 (3-4) :203-209
[10]   CLEAVAGE OF STRUCTURAL PROTEINS DURING ASSEMBLY OF HEAD OF BACTERIOPHAGE-T4 [J].
LAEMMLI, UK .
NATURE, 1970, 227 (5259) :680-+