Allergenic tropomyosins and their cross-reactivities

Yong Jeong Kyoung, Chein Soo Hong, Taisoon Yong

Research output: Contribution to journalArticle

67 Citations (Scopus)

Abstract

The ingestion or inhalation of some proteins may lead to adverse immune reactions. Allergens may trigger allergic reactions in genetically predisposed individuals when they are absorbed through the skin or make contact with mucous membranes. An allergic disease often deteriorates the quality of life and may sometimes be life-threatening due to anaphylactic shock. A number of allergens have been characterized from various multicellular organisms to date. It is thought to be reasonable to pay a special attention to the substance which is highly cross-reactive and which causes adverse responses in the molecules that are not sensitized but similar to the sensitized allergen. Tropomyosin has been described as an important food allergen in shrimp, lobster, crab, oysters, squid, and other invertebrates. Allergic reactions to shellfish and mollusks are often cross-reactive, which may be explained by the highly conserved amino acid sequences of tropomyosins among invertebrates, but vertebrate tropomyosins are not known to be allergenic. Several tropomyosins from domestic arthropods have been reported to be allergenic. Recently, it was suggested that an infection of helminthic parasites might lead to sensitization to tropomyosin and elicit allergic reactions to other invertebrates. Much effort has been made to characterize these allergenic tropomyosins from various sources. We will discuss the physicochemical characteristics and the potential application of tropomyosin for the diagnosis and therapeutics of allergic disorders.

Original languageEnglish
Pages (from-to)835-845
Number of pages11
JournalProtein and Peptide Letters
Volume13
Issue number8
DOIs
Publication statusPublished - 2006 Aug 7

Fingerprint

Tropomyosin
Allergens
Invertebrates
Hypersensitivity
Antigen-antibody reactions
Shellfish
Ostreidae
Decapodiformes
Parasitic Diseases
Arthropods
Mollusca
Anaphylaxis
Inhalation
Vertebrates
Amino Acid Sequence
Skin
Mucous Membrane
Eating
Quality of Life
Amino Acids

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry

Cite this

Kyoung, Yong Jeong ; Hong, Chein Soo ; Yong, Taisoon. / Allergenic tropomyosins and their cross-reactivities. In: Protein and Peptide Letters. 2006 ; Vol. 13, No. 8. pp. 835-845.
@article{4418616d05ff4d4ab47d649b07bc6693,
title = "Allergenic tropomyosins and their cross-reactivities",
abstract = "The ingestion or inhalation of some proteins may lead to adverse immune reactions. Allergens may trigger allergic reactions in genetically predisposed individuals when they are absorbed through the skin or make contact with mucous membranes. An allergic disease often deteriorates the quality of life and may sometimes be life-threatening due to anaphylactic shock. A number of allergens have been characterized from various multicellular organisms to date. It is thought to be reasonable to pay a special attention to the substance which is highly cross-reactive and which causes adverse responses in the molecules that are not sensitized but similar to the sensitized allergen. Tropomyosin has been described as an important food allergen in shrimp, lobster, crab, oysters, squid, and other invertebrates. Allergic reactions to shellfish and mollusks are often cross-reactive, which may be explained by the highly conserved amino acid sequences of tropomyosins among invertebrates, but vertebrate tropomyosins are not known to be allergenic. Several tropomyosins from domestic arthropods have been reported to be allergenic. Recently, it was suggested that an infection of helminthic parasites might lead to sensitization to tropomyosin and elicit allergic reactions to other invertebrates. Much effort has been made to characterize these allergenic tropomyosins from various sources. We will discuss the physicochemical characteristics and the potential application of tropomyosin for the diagnosis and therapeutics of allergic disorders.",
author = "Kyoung, {Yong Jeong} and Hong, {Chein Soo} and Taisoon Yong",
year = "2006",
month = "8",
day = "7",
doi = "10.2174/092986606777841244",
language = "English",
volume = "13",
pages = "835--845",
journal = "Protein and Peptide Letters",
issn = "0929-8665",
publisher = "Bentham Science Publishers B.V.",
number = "8",

}

Allergenic tropomyosins and their cross-reactivities. / Kyoung, Yong Jeong; Hong, Chein Soo; Yong, Taisoon.

In: Protein and Peptide Letters, Vol. 13, No. 8, 07.08.2006, p. 835-845.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Allergenic tropomyosins and their cross-reactivities

AU - Kyoung, Yong Jeong

AU - Hong, Chein Soo

AU - Yong, Taisoon

PY - 2006/8/7

Y1 - 2006/8/7

N2 - The ingestion or inhalation of some proteins may lead to adverse immune reactions. Allergens may trigger allergic reactions in genetically predisposed individuals when they are absorbed through the skin or make contact with mucous membranes. An allergic disease often deteriorates the quality of life and may sometimes be life-threatening due to anaphylactic shock. A number of allergens have been characterized from various multicellular organisms to date. It is thought to be reasonable to pay a special attention to the substance which is highly cross-reactive and which causes adverse responses in the molecules that are not sensitized but similar to the sensitized allergen. Tropomyosin has been described as an important food allergen in shrimp, lobster, crab, oysters, squid, and other invertebrates. Allergic reactions to shellfish and mollusks are often cross-reactive, which may be explained by the highly conserved amino acid sequences of tropomyosins among invertebrates, but vertebrate tropomyosins are not known to be allergenic. Several tropomyosins from domestic arthropods have been reported to be allergenic. Recently, it was suggested that an infection of helminthic parasites might lead to sensitization to tropomyosin and elicit allergic reactions to other invertebrates. Much effort has been made to characterize these allergenic tropomyosins from various sources. We will discuss the physicochemical characteristics and the potential application of tropomyosin for the diagnosis and therapeutics of allergic disorders.

AB - The ingestion or inhalation of some proteins may lead to adverse immune reactions. Allergens may trigger allergic reactions in genetically predisposed individuals when they are absorbed through the skin or make contact with mucous membranes. An allergic disease often deteriorates the quality of life and may sometimes be life-threatening due to anaphylactic shock. A number of allergens have been characterized from various multicellular organisms to date. It is thought to be reasonable to pay a special attention to the substance which is highly cross-reactive and which causes adverse responses in the molecules that are not sensitized but similar to the sensitized allergen. Tropomyosin has been described as an important food allergen in shrimp, lobster, crab, oysters, squid, and other invertebrates. Allergic reactions to shellfish and mollusks are often cross-reactive, which may be explained by the highly conserved amino acid sequences of tropomyosins among invertebrates, but vertebrate tropomyosins are not known to be allergenic. Several tropomyosins from domestic arthropods have been reported to be allergenic. Recently, it was suggested that an infection of helminthic parasites might lead to sensitization to tropomyosin and elicit allergic reactions to other invertebrates. Much effort has been made to characterize these allergenic tropomyosins from various sources. We will discuss the physicochemical characteristics and the potential application of tropomyosin for the diagnosis and therapeutics of allergic disorders.

UR - http://www.scopus.com/inward/record.url?scp=33746601347&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33746601347&partnerID=8YFLogxK

U2 - 10.2174/092986606777841244

DO - 10.2174/092986606777841244

M3 - Article

VL - 13

SP - 835

EP - 845

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

SN - 0929-8665

IS - 8

ER -