Molecular characterization of arginine kinase, an allergen from the shrimp litopenaeus vannamei

被引:144
作者
Garcia-Orozco, Karina D. [1 ]
Aispuro-Hernandez, Emmanuel [1 ]
Yepiz-Plascencia, Gloria [1 ]
Calderon-de-la-Barca, Ana Maria [1 ]
Sotelo-Mundo, Rogerio R. [1 ]
机构
[1] Ctr Invest Alimentac & Desarrollo, Aquat Mol Biol Lab, Hermosillo 83000, Sonora, Mexico
关键词
shrimp allergen; arginine kinase; cDNA cloning; Litopenaeus vannamei;
D O I
10.1159/000102610
中图分类号
R392 [医学免疫学];
学科分类号
100102 ;
摘要
Background: Consumption of seafood can produce allergic symptoms in susceptible individuals and crustacean allergies are the most frequently reported causes of allergic reactions. Methods: An allergen from the muscle of the white shrimp Litopenaeus vannamei was purified by ion exchange chromatography and identified by mass spectrometry of tryptic peptides and its specific enzymatic activity. Moreover, the corresponding full-length cDNA was obtained from an L. vannamei muscle cDNA library. Results: A 40-kDa protein was purified and identified as arginine kinase and its cDNA of 1.4 kb encoded a 356 amino acid protein. The obtained arginine kinase was recognized by IgE in serum from shrimp-allergic individuals using ELISA and immunoblotting analysis. Conclusions: This is the first allergen reported for the Pacific white shrimp species; it was named Lit v 2 and has a 96% identity to Pen m 2 from Penaeus monodon. Copyright (c) 2007 S. Karger AG, Basel.
引用
收藏
页码:23 / 28
页数:6
相关论文
共 29 条
[1]   Food allergens [J].
Aalberse, RC .
ENVIRONMENTAL TOXICOLOGY AND PHARMACOLOGY, 1997, 4 (1-2) :55-60
[2]   BASIC LOCAL ALIGNMENT SEARCH TOOL [J].
ALTSCHUL, SF ;
GISH, W ;
MILLER, W ;
MYERS, EW ;
LIPMAN, DJ .
JOURNAL OF MOLECULAR BIOLOGY, 1990, 215 (03) :403-410
[3]  
Asturias JA, 1999, J IMMUNOL, V162, P4342
[4]   Stability of food allergens and allergenicity of processed foods [J].
Besler, M ;
Steinhut, H ;
Paschke, A .
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES, 2001, 756 (1-2) :207-228
[5]   Molecular and immunological characterization of arginine kinase from the indianmeal moth, Plodia interpunctella, a novel cross-reactive invertebrate pan-allergen [J].
Binder, M ;
Mahler, V ;
Hayek, B ;
Sperr, WR ;
Schöller, M ;
Prozell, S ;
Wiedermann, G ;
Valent, P ;
Valenta, R ;
Duchêne, M .
JOURNAL OF IMMUNOLOGY, 2001, 167 (09) :5470-5477
[6]  
Blethen S, 1970, METHOD ENZYMOL, V17, P330, DOI [DOI 10.1016/0076-6879(71)17206-0, 10.1016/0076-6879(71)17206-0]
[7]   What establishes a protein as an allergen? [J].
Bredehorst, R ;
David, K .
JOURNAL OF CHROMATOGRAPHY B, 2001, 756 (1-2) :33-40
[8]  
Cheng ZJ, 2004, J ANIM SCI, V82, P1136
[9]   The use of proteotypic peptide libraries for protein identification [J].
Craig, R ;
Cortens, JP ;
Beavis, RC .
RAPID COMMUNICATIONS IN MASS SPECTROMETRY, 2005, 19 (13) :1844-1850
[10]   IDENTIFICATION OF THE MAJOR BROWN SHRIMP (PENAEUS-AZTECUS) ALLERGEN AS THE MUSCLE PROTEIN TROPOMYOSIN [J].
DAUL, CB ;
SLATTERY, M ;
REESE, G ;
LEHRER, SB .
INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY, 1994, 105 (01) :49-55