Analysis and localization of cyclophilin A found in the virions of human immunodeficiency virus type 1 MN strain

AIDS Res Hum Retroviruses. 1995 Sep;11(9):1003-6. doi: 10.1089/aid.1995.11.1003.

Abstract

Previous reports have shown that cyclophilin A (CyPA) is found to be specifically associated with human immunodeficiency virus type-1 (HIV-1) virions and is required for infectivity (Franke et al. Nature 372:359; Thali et al. Nature 372:363). We have examined CyPA associated with HIV-1MN virions. Virions from infected human lymphoid cells were analyzed by high-pressure liquid chromatography (HPLC), protein sequence, and immunoblot analysis. At least three forms of CyPA were found: an unmodified form, an N-terminally modified form, and an N-terminally modified form that migrates as a larger isoform on a reducing-SDS polyacrylamide gel. Using a protease digestion procedure, CyPA that is associated with virions was found to be located inside the viral membrane. Similar examination of SIVMne produced by HUT-78 human T cells did not detect specific incorporation of CyPA into SIV virions. Our results are consistent with the role of CyPA acting early in the infectious process of HIV-1.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Isomerases / analysis*
  • Amino Acid Isomerases / chemistry
  • Amino Acid Isomerases / metabolism
  • Amino Acids / analysis
  • Carrier Proteins / analysis*
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism
  • Cell Line
  • Chromatography, High Pressure Liquid
  • HIV-1 / chemistry*
  • HIV-1 / growth & development
  • HIV-1 / metabolism
  • Humans
  • Immunoblotting
  • Peptidylprolyl Isomerase
  • Subtilisins
  • Viral Envelope Proteins / analysis
  • Viral Envelope Proteins / metabolism

Substances

  • Amino Acids
  • Carrier Proteins
  • Viral Envelope Proteins
  • Subtilisins
  • Amino Acid Isomerases
  • Peptidylprolyl Isomerase