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Expression and antigenic analysis of the recombinant epitope of herpes simplex virus type 2 glycoprotein G |
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Abstract A fragment containing amino acid residues 561~578 of HSV-2 glycoprotein G(gG2) was obtained by PCR assembling technique, and doubly cloned into vector pET-KDO.The recombinant plasmid was transformed to BL21(DE3)plysS.Fusion protein,of molecular weight about 39,000D was highly expressed by induction of IPTG.Western-blot result showed the fusion protein had good antigenicity.After putification and digestion,the purity reached 95%.The digested purified protein was analysed by ELISA and showed good sensitivity and specificity. The recombinant protein should be useful for type-specific serodiagnosis of HSV-2.
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Received: 09 February 2007
Published: 25 September 2007
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