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

• Published in: International archives of allergy and immunology Vol. 144; no. 1; p. 23
• Main Authors: García-Orozco, Karina D, Aispuro-Hernández, Emmanuel, Yepiz-Plascencia, Gloria, Calderón-de-la-Barca, Ana María, Sotelo-Mundo, Rogerio R
• Format: Journal Article
• Language: English
• Published: Switzerland 01-01-2007
• Subjects: Allergens - chemistry; Allergens - genetics; Allergens - immunology; Amino Acid Sequence; Animals; Arginine Kinase - chemistry; Arginine Kinase - genetics; Arginine Kinase - immunology; Base Sequence; Food Hypersensitivity - enzymology; Food Hypersensitivity - immunology; Humans; Immunoglobulin E - biosynthesis; Molecular Sequence Data; Penaeidae - enzymology; Penaeidae - genetics; Penaeidae - immunology
• ISSN: 1423-0097
• DOI: 10.1159/000102610

Consumption of seafood can produce allergic symptoms in susceptible individuals and crustacean allergies are the most frequently reported causes of allergic reactions.
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.
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.
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.