If you found this site useful, please cite: Croote, D., Quake, S.R. Food allergen detection by mass spectrometry: the role of systems biology. npj Syst Biol Appl. 2016 Sep 29; 2:16022.

Allergen Targets

Shellfish


Food Matrix

Shellfish

Analysis of the allergenic proteins in black tiger prawn (Penaeus monodon) and characterization of the major allergen tropomyosin using mass spectrometry

Rahman A., Kamath S., Lopata A.L., Helleur R.J.

Rapid Communications in Mass Spectrometry (2010), 24, 16, 2462--2470 DOI: 10.1002/rcm.4664

Abstract

Crustaceans are the third most prevalent cause of food-induced anaphylaxis after peanuts and tree nuts. The severity of the allergenic proteins depends mainly on the amino acid sequence that induces production of IgE antibodies. In black tiger prawn (Penaeus monodon), the crude protein extract was profiled and its allergenic potency was examined against patient's sera. Proteins having strong immunoreactivity with patient's IgE were characterized using peptide mass fingerprinting (PMF). Tropomyosin (TM) (33 kDa), myosin light chain (20 kDa), and arginine kinase (40 kDa) were identified as allergenic proteins. Tropomyosin, the most abundant and potent allergen, was purified using ion-exchange chromatography for de novo sequencing experiments. Using bottom up tandem mass spectrometry, the full amino acid sequence was achieved by a combination of matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI) tandem mass spectrometry (QqToF). Myosin light chain and arginine kinase were also characterized, and their related peptides were de novo sequenced using the same approach. The immunological reactivity of the crude prawn extracts and purified TM samples were analyzed using a large number of patients' sera. A signature peptide was assigned for the TM protein for future quantification work of black tiger prawn TM levels in different matrices (i.e. water, air, food) in the seafood industry. Copyright © 2010 John Wiley \& Sons, Ltd.