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

Bristow, R; Byrne, J; Squirell, J; Trencher, H; Carter, T; Rodgers, B; Saman, E; Duncan, J.

J Acquir Immune Defic Syndr Hum Retrovirol ; 20(4): 334-6, 1999 Apr 01.

Article in English | MEDLINE | ID: mdl-10096576

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.

Subject(s)

Gene Products, gag/metabolism , HIV Core Protein p24/metabolism , HIV-1/metabolism , Peptidylprolyl Isomerase/metabolism , Protein Precursors/metabolism , Viral Proteins , Gene Products, gag/genetics , HIV Antigens/genetics , HIV Antigens/metabolism , HIV Core Protein p24/genetics , HIV-1/genetics , Humans , Protein Precursors/genetics , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , gag Gene Products, Human Immunodeficiency Virus

ABSTRACT

Subject(s)

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