CLEAVAGE AND PURIFICATION OF PROKARYOTICALLY EXPRESSED HIV GAG AND ENV FUSION PROTEINS FOR DETECTION OF HIV ANTIBODIES IN THE ELISA

被引:20
作者
ELLINGER, S [1 ]
MACH, M [1 ]
KORN, K [1 ]
JAHN, G [1 ]
机构
[1] UNIV ERLANGEN NURNBERG,INST KLIN & MOLEK VIROL,LOSCHGESTR 7,W-8520 ERLANGEN,GERMANY
关键词
D O I
10.1016/0042-6822(91)90097-U
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Parts of the gag p24 and the gp41 transmembrane protein of the human immunodeficiency virus HIV-1 were expressed as fusion proteins in Escherichia coli, using an expression vector carrying aa 1-375 of the lac-Z gene linked to the recognition sequence for the blood coagulation factor Xa. Fusion proteins were cleaved into the bacterial and viral portion and the viral polypeptide was purified by a molecular sieve column. The purified viral antigens were tested with 288 human sera in the enzyme-linked immunosorbent assay (ELISA) technique. Comparison with commercially available tests showed comparable sensitivity and a higher specificity of the gag/env-ELISA for borderline reactive sera. © 1991.
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收藏
页码:811 / 813
页数:3
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