Inhibition of early steps in the lentiviral replication cycle by cathelicidin host defense peptides

Retrovirology. 2005 Jan 18:2:2. doi: 10.1186/1742-4690-2-2.

Abstract

Background: The antibacterial activity of host defense peptides (HDP) is largely mediated by permeabilization of bacterial membranes. The lipid membrane of enveloped viruses might also be a target of antimicrobial peptides. Therefore, we screened a panel of naturally occurring HDPs representing different classes for inhibition of early, Env-independent steps in the HIV replication cycle. A lentiviral vector-based screening assay was used to determine the inhibitory effect of HDPs on early steps in the replication cycle and on cell metabolism.

Results: Human LL37 and porcine Protegrin-1 specifically reduced lentiviral vector infectivity, whereas the reduction of luciferase activities observed at high concentrations of the other HDPs is primarily due to modulation of cellular activity and/ or cytotoxicity rather than antiviral activity. A retroviral vector was inhibited by LL37 and Protegrin-1 to similar extent, while no specific inhibition of adenoviral vector mediated gene transfer was observed. Specific inhibitory effects of Protegrin-1 were confirmed for wild type HIV-1.

Conclusion: Although Protegrin-1 apparently inhibits an early step in the HIV-replication cycle, cytotoxic effects might limit its use as an antiviral agent unless the specificity for the virus can be improved.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-Infective Agents / pharmacology*
  • Anti-Infective Agents / toxicity
  • Antimicrobial Cationic Peptides / pharmacology*
  • Antimicrobial Cationic Peptides / toxicity
  • Cathelicidins
  • Cell Line
  • Genetic Vectors
  • Gram-Negative Bacteria / drug effects
  • Gram-Negative Bacteria / growth & development
  • Gram-Positive Cocci / drug effects
  • Gram-Positive Cocci / growth & development
  • HIV-1 / drug effects*
  • HIV-1 / physiology
  • Humans
  • Lentivirus / drug effects*
  • Lentivirus / physiology
  • Luciferases / genetics
  • Luciferases / metabolism
  • Peptides / pharmacology
  • Peptides / toxicity
  • Proteins / pharmacology*
  • Proteins / toxicity
  • Transduction, Genetic
  • Virus Replication / drug effects*

Substances

  • Anti-Infective Agents
  • Antimicrobial Cationic Peptides
  • Cathelicidins
  • Peptides
  • Proteins
  • novispirin G10
  • plectasin
  • protegrin-1
  • Luciferases