Liposomes Prevent in vitro Hemolysis Induced by Streptolysin O and Lysenin

Marcelo Ayllon, Gamid Abatchev, Andrew Bogard, Rosey Whiting, Sarah E. Hobdey, Daniel Fologea

Research output: Contribution to journalArticlepeer-review

4 Scopus citations
4 Downloads (Pure)

Abstract

The need for alternatives to antibiotics in the fight against infectious diseases has inspired scientists to focus on antivirulence factors instead of the microorganisms themselves. In this respect, prior work indicates that tiny, enclosed bilayer lipid membranes (liposomes) have the potential to compete with cellular targets for toxin binding, hence preventing their biological attack and aiding with their clearance. The effectiveness of liposomes as decoy targets depends on their availability in the host and how rapidly they are cleared from the circulation. Although liposome PEGylation may improve their circulation time, little is known about how such a modification influences their interactions with antivirulence factors. To fill this gap in knowledge, we investigated regular and long-circulating liposomes for their ability to prevent in vitro red blood cell hemolysis induced by two potent lytic toxins, lysenin and streptolysin O. Our explorations indicate that both regular and long-circulating liposomes are capable of similarly preventing lysis induced by streptolysin O. In contrast, PEGylation reduced the effectiveness against lysenin-induced hemolysis and altered binding dynamics. These results suggest that toxin removal by long-circulating liposomes is feasible, yet dependent on the particular virulence factor under scrutiny.

Original languageAmerican English
Article number364
JournalMembranes
Volume11
Issue number5
DOIs
StatePublished - 1 May 2021

Keywords

  • liposomes
  • pore-forming toxins
  • hemolysis
  • virulence factors
  • streptolysin O
  • lysenin

EGS Disciplines

  • Biochemistry, Biophysics, and Structural Biology
  • Physics

Fingerprint

Dive into the research topics of 'Liposomes Prevent in vitro Hemolysis Induced by Streptolysin O and Lysenin'. Together they form a unique fingerprint.

Cite this