Fusion Peptide Improves Stability and Bioactivity of Single Chain Antibody against Rabies Virus
| العنوان: | Fusion Peptide Improves Stability and Bioactivity of Single Chain Antibody against Rabies Virus |
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| المؤلفون: | Hualong Xi, Wei Kong, Qing Sun, Chunlai Jiang, Linqing Shi, Yanchun Yin, Tiejun Gu, Renxia Zhang, Kaixin Zhang, Yongge Wu |
| المصدر: | Journal of Microbiology and Biotechnology. 27:718-724 |
| بيانات النشر: | Journal of Microbiology and Biotechnology, 2017. |
| سنة النشر: | 2017 |
| مصطلحات موضوعية: | 0301 basic medicine, Rabies, Recombinant Fusion Proteins, Antibody Affinity, Gene Expression, Enzyme-Linked Immunosorbent Assay, Antibodies, Monoclonal, Humanized, Antibodies, Viral, Protein Engineering, medicine.disease_cause, Applied Microbiology and Biotechnology, Protein Refolding, Mice, 03 medical and health sciences, Viral Envelope Proteins, Neutralization Tests, medicine, Animals, Humans, Potency, Thermal stability, Vaccine Potency, Glycoproteins, chemistry.chemical_classification, biology, Rabies virus, General Medicine, medicine.disease, Antibodies, Neutralizing, Virology, In vitro, Drug Combinations, 030104 developmental biology, Rabies Vaccines, chemistry, Models, Animal, alpha-Synuclein, biology.protein, Female, Antibody, Glycoprotein, Fusion peptide, Half-Life, Single-Chain Antibodies, Biotechnology |
| الوصف: | The combination of rabies immunoglobulin (RIG) with a vaccine is currently effective against rabies infections, but improvements are needed. Genetic engineering antibody technology is an attractive approach for developing novel antibodies to replace RIG. In our previous study, a single-chain variable fragment, scFv57R, against rabies virus glycoprotein was constructed. However, its inherent weak stability and short half-life compared with the parent RIG may limit its diagnostic and therapeutic application. Therefore, an acidic tail of synuclein (ATS) derived from the C-terminal acidic tail of human alpha-synuclein protein was fused to the C-terminus of scFv57R in order to help it resist adverse stress and improve the stability and halflife. The tail showed no apparent effect on the preparation procedure and affinity of the protein, nor did it change the neutralizing potency in vitro. In the ELISA test of molecular stability, the ATS fusion form of the protein, scFv57R-ATS, showed an increase in thermal stability and longer half-life in serum than scFv57R. The protection against fatal rabies virus challenge improved after fusing the tail to the scFv, which may be attributed to the improved stability. Thus, the ATS fusion approach presented here is easily implemented and can be used as a new strategy to improve the stability and half-life of engineered antibody proteins for practical applications. |
| تدمد: | 1738-8872 1017-7825 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d9dadb2e2672b81ce5850b84ff6802eTest https://doi.org/10.4014/jmb.1611.11062Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....4d9dadb2e2672b81ce5850b84ff6802e |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 17388872 10177825 |
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