Human immunodeficiency virus type-1 (HIV-1) replication is unaffected by human secretory leukocyte protease inhibitor

Antiviral Res. 1996 Mar;29(2-3):269-77. doi: 10.1016/0166-3542(95)00907-8.

Abstract

Human secretory leukocyte protease inhibitor (SLPI), a serine protease inhibitor found concentrated in secretory fluids, has been postulated to participate in the body's natural defense against infection by the human immunodeficiency virus type-1 (HIV-1) by affecting trypsin-like enzymes on the surface of target cells. SLPI was evaluated for potential antiviral activity against laboratory, clinical and monocytotropic strains of HIV-1 in human T-cell lines, peripheral blood lymphocytes and monocyte/macrophage cultures. SLPI was tested in a single cycle of infection assay and under conditions in which SLPI was preincubated both with target cells and with virus and then maintained during the virus-to-cell adsorption phase and throughout the entire culture period. However, SLPI did not exert anti-HIV activity under any experimental conditions, and mechanistic studies showed SLPI to have no inhibitory activity on HIV-1 binding, reverse transcriptase or protease. Thus, SLPI exhibited no suggestive anti-HIV-1 activity.

Publication types

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

MeSH terms

  • Cell Line
  • Cells, Cultured
  • HIV Core Protein p24 / analysis
  • HIV-1 / drug effects*
  • HIV-1 / metabolism
  • HIV-1 / physiology
  • HeLa Cells
  • Humans
  • Leukocytes / enzymology
  • Proteinase Inhibitory Proteins, Secretory
  • Proteins / pharmacology*
  • Recombinant Proteins / pharmacology
  • Secretory Leukocyte Peptidase Inhibitor
  • Serine Proteinase Inhibitors / pharmacology*
  • Time Factors
  • Virus Replication / drug effects

Substances

  • HIV Core Protein p24
  • Proteinase Inhibitory Proteins, Secretory
  • Proteins
  • Recombinant Proteins
  • SLPI protein, human
  • Secretory Leukocyte Peptidase Inhibitor
  • Serine Proteinase Inhibitors