TY - JOUR
T1 - Role of tropomyosin in silkworm allergy
AU - Jeong, Kyoung Yong
AU - Han, In Soo
AU - Lee, June Yong
AU - Park, Kyung Hee
AU - Lee, Jae Hyun
AU - Park, Jung Won
N1 - Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2017
Y1 - 2017
N2 - Silkworm pupae are widely consumed in Asian countries and allergic reactions following consumption have been described. However, false-positive responses in skin prick allergy tests or non-specifc immunoglobulin E (IgE) responses to total extract of silkworm pupa make diagnosis diffcult. Although improved allergy diagnosis is required, molecular characterization of silkworm allergens has not been performed to date, except for Bomb m 1, an arginine kinase. This study aimed to evaluate the allergenicity of tropomyosin, a well-established invertebrate pan-allergen, from silkworm pupa. The silkworm tropomyosin gene was cloned by reverse transcription and polymerase chain reaction, and the protein was overexpressed in Escherichia coli and purifed by affnity chromatography using Nickel-resin. IgE reactivity of the recombinant protein was examined by ELISA and competitive inhibition analyses. Silkworm pupa tropomyosin shared 73.5-92.3% amino acid sequence identity with previously identifed allergenic tropomyosins. Sera from eight of 15 patients with silkworm allergy (53.3%) exhibited binding of IgE to the recombinant protein. However, recombinant protein was able to inhibit less than 10% of IgE reactivity to silkworm pupa extract. Of the eight sera tested, six that specifcally reacted with silkworm tropomyosin also demonstrated IgE reactivity to shrimp and crab. In the present study, specifc IgE to silkworm tropomyosin was detected in patients with silkworm allergy, suggesting that it may be useful in diagnosis of allergy to silkworm pupa.
AB - Silkworm pupae are widely consumed in Asian countries and allergic reactions following consumption have been described. However, false-positive responses in skin prick allergy tests or non-specifc immunoglobulin E (IgE) responses to total extract of silkworm pupa make diagnosis diffcult. Although improved allergy diagnosis is required, molecular characterization of silkworm allergens has not been performed to date, except for Bomb m 1, an arginine kinase. This study aimed to evaluate the allergenicity of tropomyosin, a well-established invertebrate pan-allergen, from silkworm pupa. The silkworm tropomyosin gene was cloned by reverse transcription and polymerase chain reaction, and the protein was overexpressed in Escherichia coli and purifed by affnity chromatography using Nickel-resin. IgE reactivity of the recombinant protein was examined by ELISA and competitive inhibition analyses. Silkworm pupa tropomyosin shared 73.5-92.3% amino acid sequence identity with previously identifed allergenic tropomyosins. Sera from eight of 15 patients with silkworm allergy (53.3%) exhibited binding of IgE to the recombinant protein. However, recombinant protein was able to inhibit less than 10% of IgE reactivity to silkworm pupa extract. Of the eight sera tested, six that specifcally reacted with silkworm tropomyosin also demonstrated IgE reactivity to shrimp and crab. In the present study, specifc IgE to silkworm tropomyosin was detected in patients with silkworm allergy, suggesting that it may be useful in diagnosis of allergy to silkworm pupa.
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U2 - 10.3892/mmr.2017.6373
DO - 10.3892/mmr.2017.6373
M3 - Article
C2 - 28339033
AN - SCOPUS:85018692728
VL - 15
SP - 3264
EP - 3270
JO - Molecular Medicine Reports
JF - Molecular Medicine Reports
SN - 1791-2997
IS - 5
ER -