Melittin-loaded immunoliposomes against viral surface proteins, a new approach to antiviral therapy

Antiviral Res. 2013 Feb;97(2):218-21. doi: 10.1016/j.antiviral.2012.12.004. Epub 2012 Dec 20.

Abstract

In this study, melittin, a well-characterized pore-forming lytic amphiphilic peptide susceptible to be vehiculized in lipid membranes, has been utilized to study their antiviral properties. For this purpose, an assay based on melittin loaded-immunoliposomes previously described by our group was adapted to antiviral purposes by means of monoclonal antibodies targeting the surface G glycoprotein of the fish viral haemorrhagic septicemia rhabdovirus (VHSV). We also studied the antiviral action of these immunoliposomes in vitro and the results showed that they are capable of inhibiting the VHSV infectivity by 95.2% via direct inactivation of the virus. Furthermore, the inhibition of the infectivity when treatments were added at different times post-infection and the analysis of the infection foci sizes suggested altogether that they also act by reducing the VHSV spread in cell culture and by killing the infected cells which express the G glycoprotein in their plasmatic membranes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antiviral Agents / pharmacology*
  • Cell Line
  • Fishes
  • Liposomes / metabolism*
  • Melitten / pharmacology*
  • Membrane Proteins / antagonists & inhibitors*
  • Microbial Sensitivity Tests
  • Microbial Viability / drug effects
  • Novirhabdovirus / drug effects*
  • Viral Proteins / antagonists & inhibitors*
  • Virus Inactivation

Substances

  • Antiviral Agents
  • Liposomes
  • Membrane Proteins
  • Viral Proteins
  • Melitten