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Expression and purification of human respiratory syncytial virus recombinant fusion protein |
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| Authors: | Arcuri Helen A Apponi Luciano H Valentini Sandro R Durigon Edison L de Azevedo Walter F Fossey Marcelo A Rahal Paula de Souza Fatima P |
| Affiliation: | aInstituto de Biociências, Letras e Ciências Exatas/UNESP, Rua Cristóvão Colombo, 2265, São José do Rio Preto, CEP 15054-000, SJRP-SP, Brazil;bFaculdade de Ciências Farmacêuticas/UNESP, 14801-902 Araraquara-SP, Brazil;cInstituto de Ciências Biomédicas/USP, 05508-900 São Paulo-SP, Brazil;dFaculdade de Biociências/PUCRGS, Porto Alegre-RS, 90619-900, Brazil |
| Abstract: | The Human Respiratory Syncytial Virus (HRSV) fusion protein (F) was expressed in Escherichia coli BL21A using the pET28a vector at 37 °C. The protein was purified from the soluble fraction using affinity resin. The structural quality of the recombinant fusion protein and the estimation of its secondary structure were obtained by circular dichroism. Structural models of the fusion protein presented 46% of the helices in agreement with the spectra by circular dichroism analysis. There are only few studies that succeeded in expressing the HRSV fusion protein in bacteria. This is a report on human fusion protein expression in E. coli and structure analysis, representing a step forward in the development of fusion protein F inhibitors and the production of antibodies. |
| Keywords: | Fusion protein Purification Dichroism analysis Molecular modeling Expression |
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