Gnathostoma spinigerum: Molecular cloning, expression and characterization of the cyclophilin protein

In this study, a cDNA encoding cyclophilin (CyP) of Gnathostoma spinigerum was cloned into a prokaryotic expression vector and expressed in Escherichia coli. The predicted molecular mass of the putative protein was 18.6. kDa, and the deduced amino acid sequence had 86, 84.8, 81.3 and 77.2% identity...

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Main Authors: Laummaunwai P., Intapan P.M., Wongkham C., Lulitanond V., Tayapiwatana C., Maleewong W.
格式: Article
語言:English
出版: 2014
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http://cmuir.cmu.ac.th/handle/6653943832/849
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spelling th-cmuir.6653943832-8492014-08-29T09:02:14Z Gnathostoma spinigerum: Molecular cloning, expression and characterization of the cyclophilin protein Laummaunwai P. Intapan P.M. Wongkham C. Lulitanond V. Tayapiwatana C. Maleewong W. In this study, a cDNA encoding cyclophilin (CyP) of Gnathostoma spinigerum was cloned into a prokaryotic expression vector and expressed in Escherichia coli. The predicted molecular mass of the putative protein was 18.6. kDa, and the deduced amino acid sequence had 86, 84.8, 81.3 and 77.2% identity with the CyP of Dirofilaria immitis, Brugia malayi, Onchocerca volvulus and Caenorhabditis elegans, respectively. A prediction of linear B-cell epitopes with high hydrophilicity and immunoblotting results indicated that the recombinant CyP has antigenicity to humans. The recombinant CyP protein reacted with human gnathostomiasis sera but not with other parasitosis or healthy control sera, suggesting that it might be useful for the serodiagnosis of human gnathostomiasis. © Elsevier Inc. 2014-08-29T09:02:14Z 2014-08-29T09:02:14Z 2010 Article 144894 10.1016/j.exppara.2010.06.004 20594967 EXPAA http://www.scopus.com/inward/record.url?eid=2-s2.0-80054913334&partnerID=40&md5=d408b17ff77c771cbdd99dee9cba2498 http://cmuir.cmu.ac.th/handle/6653943832/849 English
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
language English
description In this study, a cDNA encoding cyclophilin (CyP) of Gnathostoma spinigerum was cloned into a prokaryotic expression vector and expressed in Escherichia coli. The predicted molecular mass of the putative protein was 18.6. kDa, and the deduced amino acid sequence had 86, 84.8, 81.3 and 77.2% identity with the CyP of Dirofilaria immitis, Brugia malayi, Onchocerca volvulus and Caenorhabditis elegans, respectively. A prediction of linear B-cell epitopes with high hydrophilicity and immunoblotting results indicated that the recombinant CyP has antigenicity to humans. The recombinant CyP protein reacted with human gnathostomiasis sera but not with other parasitosis or healthy control sera, suggesting that it might be useful for the serodiagnosis of human gnathostomiasis. © Elsevier Inc.
format Article
author Laummaunwai P.
Intapan P.M.
Wongkham C.
Lulitanond V.
Tayapiwatana C.
Maleewong W.
spellingShingle Laummaunwai P.
Intapan P.M.
Wongkham C.
Lulitanond V.
Tayapiwatana C.
Maleewong W.
Gnathostoma spinigerum: Molecular cloning, expression and characterization of the cyclophilin protein
author_facet Laummaunwai P.
Intapan P.M.
Wongkham C.
Lulitanond V.
Tayapiwatana C.
Maleewong W.
author_sort Laummaunwai P.
title Gnathostoma spinigerum: Molecular cloning, expression and characterization of the cyclophilin protein
title_short Gnathostoma spinigerum: Molecular cloning, expression and characterization of the cyclophilin protein
title_full Gnathostoma spinigerum: Molecular cloning, expression and characterization of the cyclophilin protein
title_fullStr Gnathostoma spinigerum: Molecular cloning, expression and characterization of the cyclophilin protein
title_full_unstemmed Gnathostoma spinigerum: Molecular cloning, expression and characterization of the cyclophilin protein
title_sort gnathostoma spinigerum: molecular cloning, expression and characterization of the cyclophilin protein
publishDate 2014
url http://www.scopus.com/inward/record.url?eid=2-s2.0-80054913334&partnerID=40&md5=d408b17ff77c771cbdd99dee9cba2498
http://cmuir.cmu.ac.th/handle/6653943832/849
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