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Expression and immune characterization of a novel enzyme, protein arginine methyltransferase 1, from Schistosoma japonicum
Protein arginine methyltransferase 1 (PRMT1) is an arginine-specific protein methyltransferase that methylates a number of proteins involved in transcription and RNA metabolism in all parasitic helminths, including the human blood fluke, Schistosoma japonicum. To characterize the role of PRMT1 in th...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3932173/ https://www.ncbi.nlm.nih.gov/pubmed/24343727 http://dx.doi.org/10.1007/s00436-013-3723-6 |
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author | Diao, Wei Zhou, Hejun Pan, Wei Liu, Haipeng Shen, Yujuan Xu, Yuxin Li, Xiaohong Cao, Jianping |
author_facet | Diao, Wei Zhou, Hejun Pan, Wei Liu, Haipeng Shen, Yujuan Xu, Yuxin Li, Xiaohong Cao, Jianping |
author_sort | Diao, Wei |
collection | PubMed |
description | Protein arginine methyltransferase 1 (PRMT1) is an arginine-specific protein methyltransferase that methylates a number of proteins involved in transcription and RNA metabolism in all parasitic helminths, including the human blood fluke, Schistosoma japonicum. To characterize the role of PRMT1 in the development of S. japonicum and to investigate its influence on parasite–host interactions, we cloned and expressed the protein from an existing cDNA library. We report that the clone encoded a polypeptide comprising 360 amino acids with a predictive Mr of 42 kDa. Bioinformatic analyses predicted that there were many potential B cell epitopes and T cell epitopes associated with SjcPRMT1, suggesting it is a potential candidate molecule for vaccine development. The purified recombinant protein of S. japonicum (Chinese strain) (rSjcPRMT1) was found to be immunogenic, eliciting a high antibody titer in mice. Moreover, Western blot analysis revealed that the protein could be recognized by the sera of infected mice. Using flow cytometry, we showed that rSjcPRMT1 slightly upregulated the expression of CD40, CD80, CD86, and MHC-II molecules of mouse bone marrow-derived dendritic cell (BMDC), indicating that rSjcPRMT1 could induce mouse BMDC to mature and, therefore, activate their immune response. Overall, our findings provide evidence that rSjcPRMT1 could serve as an effective candidate molecule for the development of a vaccine against infection with S. japonicum. |
format | Online Article Text |
id | pubmed-3932173 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-39321732014-02-28 Expression and immune characterization of a novel enzyme, protein arginine methyltransferase 1, from Schistosoma japonicum Diao, Wei Zhou, Hejun Pan, Wei Liu, Haipeng Shen, Yujuan Xu, Yuxin Li, Xiaohong Cao, Jianping Parasitol Res Original Paper Protein arginine methyltransferase 1 (PRMT1) is an arginine-specific protein methyltransferase that methylates a number of proteins involved in transcription and RNA metabolism in all parasitic helminths, including the human blood fluke, Schistosoma japonicum. To characterize the role of PRMT1 in the development of S. japonicum and to investigate its influence on parasite–host interactions, we cloned and expressed the protein from an existing cDNA library. We report that the clone encoded a polypeptide comprising 360 amino acids with a predictive Mr of 42 kDa. Bioinformatic analyses predicted that there were many potential B cell epitopes and T cell epitopes associated with SjcPRMT1, suggesting it is a potential candidate molecule for vaccine development. The purified recombinant protein of S. japonicum (Chinese strain) (rSjcPRMT1) was found to be immunogenic, eliciting a high antibody titer in mice. Moreover, Western blot analysis revealed that the protein could be recognized by the sera of infected mice. Using flow cytometry, we showed that rSjcPRMT1 slightly upregulated the expression of CD40, CD80, CD86, and MHC-II molecules of mouse bone marrow-derived dendritic cell (BMDC), indicating that rSjcPRMT1 could induce mouse BMDC to mature and, therefore, activate their immune response. Overall, our findings provide evidence that rSjcPRMT1 could serve as an effective candidate molecule for the development of a vaccine against infection with S. japonicum. Springer Berlin Heidelberg 2013-12-17 2014 /pmc/articles/PMC3932173/ /pubmed/24343727 http://dx.doi.org/10.1007/s00436-013-3723-6 Text en © The Author(s) 2013 https://creativecommons.org/licenses/by/2.0/ Open Access This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. |
spellingShingle | Original Paper Diao, Wei Zhou, Hejun Pan, Wei Liu, Haipeng Shen, Yujuan Xu, Yuxin Li, Xiaohong Cao, Jianping Expression and immune characterization of a novel enzyme, protein arginine methyltransferase 1, from Schistosoma japonicum |
title | Expression and immune characterization of a novel enzyme, protein arginine methyltransferase 1, from Schistosoma japonicum |
title_full | Expression and immune characterization of a novel enzyme, protein arginine methyltransferase 1, from Schistosoma japonicum |
title_fullStr | Expression and immune characterization of a novel enzyme, protein arginine methyltransferase 1, from Schistosoma japonicum |
title_full_unstemmed | Expression and immune characterization of a novel enzyme, protein arginine methyltransferase 1, from Schistosoma japonicum |
title_short | Expression and immune characterization of a novel enzyme, protein arginine methyltransferase 1, from Schistosoma japonicum |
title_sort | expression and immune characterization of a novel enzyme, protein arginine methyltransferase 1, from schistosoma japonicum |
topic | Original Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3932173/ https://www.ncbi.nlm.nih.gov/pubmed/24343727 http://dx.doi.org/10.1007/s00436-013-3723-6 |
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