Human Cyclophilin Has a Significantly Higher Affinity for HIV-1 Recombinant p55 Than p24

J Acquir Immune Defic Syndr Hum Retrovirol. 1999 Apr 1;20(4):334-6. doi: 10.1097/00042560-199904010-00002.

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.

MeSH terms

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

Substances

  • Gene Products, gag
  • HIV Antigens
  • HIV Core Protein p24
  • Protein Precursors
  • Recombinant Fusion Proteins
  • Viral Proteins
  • gag Gene Products, Human Immunodeficiency Virus
  • gag protein p26, Human immunodeficiency virus
  • p17 protein, Human Immunodeficiency Virus Type 1
  • p55 gag precursor protein, Human immunodeficiency virus 1
  • Peptidylprolyl Isomerase