Construction of Soluble Mamu-B*1703, a Class I Major Histocompatibility Complex of Chinese Rhesus Macaques, Monomer and Tetramer Loaded with a Simian Immunodeficiency Virus Peptide
| العنوان: | Construction of Soluble Mamu-B*1703, a Class I Major Histocompatibility Complex of Chinese Rhesus Macaques, Monomer and Tetramer Loaded with a Simian Immunodeficiency Virus Peptide |
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| المؤلفون: | Xiaoying Wang, Dong-Yun Ouyang, He Guo, Huanjing Shi, Qi Gao, Li-Hui Xu, Xian-Hui He |
| المصدر: | Cellular & Molecular Immunology. 6:117-122 |
| بيانات النشر: | Springer Science and Business Media LLC, 2009. |
| سنة النشر: | 2009 |
| مصطلحات موضوعية: | China, Protein Folding, Genetic Vectors, Immunology, India, CD8-Positive T-Lymphocytes, Protein Engineering, medicine.disease_cause, Major histocompatibility complex, Macaque, Article, Epitope, Tetramer, biology.animal, MHC class I, medicine, Animals, Immunology and Allergy, Antigens, Viral, biology, Immunodominant Epitopes, Histocompatibility Antigens Class I, Simian immunodeficiency virus, Macaca mulatta, Virology, Infectious Diseases, Biotinylation, biology.protein, Simian Immunodeficiency Virus, Protein Multimerization, Peptides, CD8, Protein Binding |
| الوصف: | Chinese-descent rhesus macaques have become more prevalent for HIV infection and vaccine investigation than Indian-origin macaques. Most of the currently available data and reagents such as major histocompatibility complex (MHC) class I tetramers, however, were derived from Indian-origin macaques due to the dominant use of these animals in history. Although there are significant differences in the immunogenetic background between the two macaque populations, they share a few of common MHC class I alleles. We reported in this study the procedure for preparation of a soluble Mamu-B*1703 (a MHC class I molecule of Chinese macaques) monomer and tetramer loaded with a dominant simian immunodeficiency virus (SIV) epitope IW9 (IRYPKTFGW) that was identified to be Mamu-B*1701-restricted in Indian macaques. The DNA fragment encoding the Mamu-B*1703 extracellular domain fused with a BirA substrate peptide (BSP) was amplified from a previously cloned cDNA and inserted into a prokaratic expression vector. In the presence of the antigenic peptide IW9 and light chain beta2-microglobulin, the expressed heavy chain was refolded into a soluble monomer. After biotinylation, four monomers were polymerized as a tetramer by phycoerythrin-conjugated streptavidin. The tetramer, having been confirmed to have the right conformation, was a potential tool for investigation of antigen-specific CD8(+) T-lymphocytes in SIV vaccine models of Chinese macaques. And our results also suggested that some antigenic peptides reported in Indian-origin macaques could be directly recruited as ligands for construction of Chinese macaque MHC tetramers. |
| تدمد: | 2042-0226 1672-7681 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec31d49b8907ae467c463490afe20cd0 https://doi.org/10.1038/cmi.2009.16 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....ec31d49b8907ae467c463490afe20cd0 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 20420226 16727681 |
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