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Title 

Overexpression and simple purification of human immunodeficiency virus-1 gag epitope derived from a recombinant antigen in E. coli and its use in ELISA

Authors 

Mi Jin SohnYoung Hae ChongJi Eun ChangYoung Ik Lee

Publisher 

Elsevier

Issue Date 

1994

Citation 

Journal of Biotechnology, vol. 34, no. 0, pp. 149-155

Keywords 

Gag3 purificationHuman immunodeficency virus-1epitopevirus antigenvirus proteinenzyme linked immunosorbent assayescherichia coligene expressionhuman immunodeficiency virus 1molecular cloning

Abstract 

To develop a test for diagnosis of human immunodeficiency virus-1 (HIV-1) exposure sensitivity, a part of the gag gene was cloned and expressed in Escherichia coli, using expression vectors containing a trp promoter. The immunoreactivity of recombinant protein was determined using HIV-1 specific antibodies in a Western blot analysis. The recombinant plasmid, pYHCgag3, gag gene was fused to the trpE' gene linked to the hydroxylamine (HA) cleavage recognition sequence which was induced to overexpress a core antigen (gag a.a. 121-398 from plasmid BH10) as fusion protein in the form of insoluble inclusion body. Recombinant gag was purified by a simple single step purification procedure. After partial purification of inclusion bodies and subject to the HA-cleavage treatment, gag protein was further purified to homogeneity using DEAE-Sepharose chromatography. The purified core antigen offered reliable results with high sensitivity and specificity for identification of HIV-1 antibodies when tested in the enzyme-linked immunosorbent assay (ELISA). These results suggest that mass production of recombinant core antigen will provide a valuable resource to HIV-1 serodiagnostics for the screening of large groups of blood donors to prevent HIV-1 infection.

ISSN 

0168-1656

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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