Human cyclophilin has a significantly higher affinity for HIV-1 recombinant p55 than p24.

R Bristow, J Byrne, J Squirell, H Trencher, T Carter, B Rodgers, E Saman, J Duncan
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引用次数: 17

Abstract

The ability of cyclophilin to bind a panel of recombinant HIV-gag proteins was assessed using sensitive, quantitative, sandwich enzyme-linked immunosorbant assays (ELISAs). Significantly higher binding to cyclophilin was observed when recombinants contained at least 12 carboxy-terminal amino acids of p17 in addition to p24 sequences. These results indicate that the carboxy-terminus of p17 is important for optimal binding of cyclophilin to p24 and support the theory that cyclophilin acts on the uncleaved HIV-1 gag (p17-p24) precursor.

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人亲环蛋白对HIV-1重组蛋白p55的亲和力明显高于p24。
采用敏感、定量、夹心酶联免疫吸附试验(elisa)评估亲环蛋白结合重组HIV-gag蛋白的能力。除了p24序列外,当重组体含有至少12个p17的羧基末端氨基酸时,观察到与亲环蛋白的结合显著提高。这些结果表明,p17的羧基末端对于亲环蛋白与p24的最佳结合很重要,并支持亲环蛋白作用于未裂解的HIV-1 gag (p17-p24)前体的理论。
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