Expression and purification of fusion protein containing the segment of glycoprotein G of RSV and the serum albumin-binding region of streptococcal protein G(BB)
SONG Yan
WANG Xiliang
Abstract：Objective To construct a prokaryotic expression system for the amino-acid region 130-230 of glycoprotein G and the serum albumin-binding region of SPG,and search an appropriate induction and purification conditions for gaining soluble fusion pro tein.Methods G2Na gene and BB gene were amplified by PCR with cDNA of RSV and DNA of streptococcal genome as templates,respectively.The recombinant expression plasmid PET32a(BBG2Na)containing Thx-BB-G2Na fusion gene was constructed by recombinant DNA technique,and then transformed into Escherichia coli BL21(DE3).The expression product was purified by affinity chromatography.Results The expression level of Thx-BB-G2Na fusion protein was about 68%of total cellular protein.The Thx-G2Na-BB fusion protein existed in suspension of the lysis solution of B121(DE3).After purification,the purity of fusion protein in elution was more than 90%.Conclusion The Thx-G2Na-BB could be used as an antigen for screening recombinant protein vaccine against RSV.
Keywords：respiratory syncytial virusserum albumin-binding region of streptococcal proteinprokaryotic expressionprotein purification
Publication Date：2009-01-01
Online Publishing Date：2025-08-15(First online date of this platform, not the publication date of the document)
Pages：3( 722-724 )