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Analysis of amino acid sequence variations and immunoglobulin E-binding epitopes of German cockroach tropomyosin

Authors
 Kyoung Yong Jeong  ;  Jongweon Lee  ;  Tai-Soon Yong  ;  Chein-Soo Hong  ;  Han-Il Ree  ;  In-Yong Lee 
Citation
 CLINICAL AND DIAGNOSTIC LABORATORY IMMUNOLOGY , Vol.11(5) : 874-878, 2004 
Journal Title
CLINICAL AND DIAGNOSTIC LABORATORY IMMUNOLOGY
ISSN
 1071-412X 
Issue Date
2004
MeSH
Alternative Splicing* ; Amino Acid Sequence ; Animals ; Antigen-Antibody Reactions ; Cockroaches/immunology* ; Cross Reactions/genetics ; Cross Reactions/immunology ; DNA, Complementary ; Immunodominant Epitopes/genetics* ; Immunoglobulin E/immunology* ; Protein Isoforms ; Sequence Analysis, Protein* ; Tropomyosin/genetics ; Tropomyosin/immunology*
Abstract
The allergenicities of tropomyosins from different organisms have been reported to vary. The cDNA encoding German cockroach tropomyosin (Bla g 7) was isolated, expressed, and characterized previously. In the present study, the amino acid sequence variations in German cockroach tropomyosin were analyzed in order to investigate its influence on allergenicity. We also undertook the identification of immunodominant peptides containing immunoglobulin E (IgE) epitopes which may facilitate the development of diagnostic and immunotherapeutic strategies based on the recombinant proteins. Two-dimensional gel electrophoresis and immunoblot analysis with mouse anti-recombinant German cockroach tropomyosin serum was performed to investigate the isoforms at the protein level. Reverse transcriptase PCR (RT-PCR) was applied to examine the sequence diversity. Eleven different variants of the deduced amino acid sequences were identified by RT-PCR. German cockroach tropomyosin has only minor sequence variations that did not seem to affect its allergenicity significantly. These results support the molecular basis underlying the cross-reactivities of arthropod tropomyosins. Recombinant fragments were also generated by PCR, and IgE-binding epitopes were assessed by enzyme-linked immunosorbent assay. Sera from seven patients revealed heterogeneous IgE-binding responses. This study demonstrates multiple IgE-binding epitope regions in a single molecule, suggesting that full-length tropomyosin should be used for the development of diagnostic and therapeutic reagents.
Files in This Item:
T200403989.pdf Download
DOI
10.1128/CDLI.11.5.874-878.2004
Appears in Collections:
1. College of Medicine (의과대학) > Research Institute (부설연구소) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Tropica Medicine (열대의학교실) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Internal Medicine (내과학교실) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Thoracic and Cardiovascular Surgery (흉부외과학교실) > 1. Journal Papers
Yonsei Authors
Yong, Tai Soon(용태순) ORCID logo https://orcid.org/0000-0002-3445-0769
Lee, In Yong(이인용)
Lee, Jong Weon(이종원)
Ree, Han Il(이한일)
Jeong, Kyoung Yong(정경용) ORCID logo https://orcid.org/0000-0001-9887-1426
Hong, Chein Soo(홍천수)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/112883
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