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Short Communication: 1. Allergens, Epitopes and Allergen Recognition

Characterization of Recombinant Shrimp Allergen Pen a 1 (Tropomyosin)

Reese G. · Jeoung B.-J. · Daul C.B. · Lehrer S.B.

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Clinical Immunology and Allergy Section, Department of Medicine, Tulane University Medical Center, New Orleans, La., USA

Related Articles for ""

Int Arch Allergy Immunol 1997;113:240–242

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Article / Publication Details

First-Page Preview
Abstract of Short Communication: 1. Allergens, Epitopes and Allergen Recognition

Published online: September 04, 2009
Issue release date: 1997

Number of Print Pages: 3
Number of Figures: 0
Number of Tables: 0

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: https://www.karger.com/IAA

Abstract

Tropomyosin (Pen a 1) from brown shrimp, Penaeus aztecus, has been identified as the only major shrimp allergen. Since beef, pork and chicken are other tropo-myosin-containing foods that are not very allergenic, tropomyosins can serve to investigate the contribution of the structural properties of a protein to its allergenicity. The aim of this study was to determine the primary structure of Pen a 1 and to identify IgE-binding epitopes. The screening of a unidirectional expression cDNA library from shrimp tail muscle with the Pen-a-1-specific monoclonal antibody 4.9.5 resulted in 4 positive Escherichia coli clones. Immunoblot analysis with human sera from shrimp-allergic subjects demonstrated IgE binding of all 4 recombinant shrimp proteins. Three of 4 expressed recombinant proteins have a molecular weight of approximately 36 kD, consistent with the molecular weight of natural Pen a 1. The DNA sequence analysis identified these recombinant shrimp proteins as tropomyosin and could be aligned with the sequence of greasyback shrimp (Metapenaeus ensis) tropomyosin (Met e 1). In order to characterize contiguous IgE-binding epitopes of Pen a 1, a peptide library (Novagen epitope mapping system) expressing 10–30 amino-acid-residue-long recombinant Pen a 1 peptides was constructed and screened with human IgE. Four recombinant, IgE-reactive Pen a 1 peptides were selected and sequenced. They show various degrees of sequence identity with tropomyosins of other arthropods, such as fruitfly and house dust mite, helminths and vertebrates.

© 1997 S. Karger AG, Basel


Article / Publication Details

First-Page Preview
Abstract of Short Communication: 1. Allergens, Epitopes and Allergen Recognition

Published online: September 04, 2009
Issue release date: 1997

Number of Print Pages: 3
Number of Figures: 0
Number of Tables: 0

ISSN: 1018-2438 (Print)
eISSN: 1423-0097 (Online)

For additional information: https://www.karger.com/IAA


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