pH dependence of listeriolysin O aggregation and pore-forming ability (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• pH dependence of listeriolysin O aggregation and pore-forming ability (Articolo in rivista) (literal)

Anno

• 2012-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1111/j.1742-4658.2011.08405.x (literal)

Alternative label

• Bavdek A, Kostanjšek R, Antonini V, Lakey JH, Dalla Serra M, Gilbert RJ, Anderluh G (2012)
  pH dependence of listeriolysin O aggregation and pore-forming ability
  in The FEBS journal (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Bavdek A, Kostanjšek R, Antonini V, Lakey JH, Dalla Serra M, Gilbert RJ, Anderluh G (literal)

Pagina inizio

• 126 (literal)

Pagina fine

• 141 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 279 (literal)

Rivista

• ?The ?FEBS journal (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 1 (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Natl Inst Chem, Ljubljana 1000, Slovenia Univ Ljubljana, Dept Biol, Biotech Fac, Ljubljana 61000, Slovenia CNR Inst Biophys, Unit Trento, Trento Povo, Italy Bruno Kessler Fdn, Trento Povo, Italy Newcastle Univ, Newcastle Upon Tyne, Tyne & Wear, England Univ Oxford, Wellcome Trust Ctr Human Genet, Div Struct Biol, Oxford, England (literal)

Titolo

• pH dependence of listeriolysin O aggregation and pore-forming ability (literal)

Abstract

• Listeriolysin O (LLO) is the major factor implicated in the escape of Listeria monocytogenes from the phagolysosome. It is the only representative of cholesterol-dependent cytolysins that exhibits pH-dependent activity. Despite intense studies of LLO pH-dependence, this feature of the toxin still remains incompletely explained. Here we used fluorescence and CD spectroscopy to show that the structure of LLO is not detectably affected by pH at room temperature. We observed slightly altered haemolytic and permeabilizing activities at different pH values, which we relate to reduced binding of LLO to the lipid membranes. However, alkaline pH and elevated temperatures caused rapid denaturation of LLO. Aggregates of the toxin were able to bind Congo red and Thioflavin T dyes and were visible under transmission electron microscopy as large, amorphous, micrometer-sized assemblies. The aggregates had the biophysical properties of amyloid. Analytical ultracentrifugation indicated dimerization of the protein in acidic conditions, which protects the protein against premature denaturation in the phagolysosome, where toxin activity takes place. We therefore suggest that LLO spontaneously aggregates at the neutral pH found in the host cell cytosol and that this is a major mechanism of LLO inactivation (literal)

Prodotto di

• Istituto di biofisica (IBF) (Istituto)
• Membrane biologiche, complessi macromolecolari e imaging biomolecolare (MD.P01.028.001) (Modulo)

Autore CNR

• MAURO DALLA SERRA (Unità di personale interno)
• VALERIA ANTONINI (Persona)

Incoming links:

Prodotto

• Istituto di biofisica (IBF) (Istituto)
• Membrane biologiche, complessi macromolecolari e imaging biomolecolare (MD.P01.028.001) (Modulo)

Autore CNR di

• MAURO DALLA SERRA (Unità di personale interno)
• VALERIA ANTONINI (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• ?The ?FEBS journal (Rivista)