Results 91 to 100 of about 1,388 (159)

Tracking cholesterol/sphingomyelin-rich membrane domains with the ostreolysin A-mCherry protein.

PLoS ONE, 2014
Ostreolysin A (OlyA) is an ∼15-kDa protein that has been shown to bind selectively to membranes rich in cholesterol and sphingomyelin. In this study, we investigated whether OlyA fluorescently tagged at the C-terminal with mCherry (OlyA-mCherry) labels ...
Matej Skočaj, Nataša Resnik, Maja Grundner, Katja Ota, Nejc Rojko, Vesna Hodnik, Gregor Anderluh, Andrzej Sobota, Peter Maček, Peter Veranič, Kristina Sepčić   +10 more
doaj   +1 more source

Dynamic Gene Expression Mitigates Mutational Escape in Lysis-Driven Bacteria Cancer Therapy

BioDesign Research
Engineered bacteria have the potential to deliver therapeutic payloads directly to tumors, with synthetic biology enabling precise control over therapeutic release in space and time.
Filippo Liguori, Nicola Pellicciotta, Edoardo Milanetti, Sophia Xi Windemuth, Giancarlo Ruocco, Roberto Di Leonardo, Tal Danino   +6 more
doaj   +1 more source

Perfringolysin O pore formation dynamics: from soluble monomer to membrane insertion and beyond

, 2022
Perfringolysin O (PFO) is a cholesterol dependent cytolysin (CDC) secreted by Clostridium perfringens, which forms pores in cholesterol containing membranes. CDCs are part of the larger Membrane attack complex-Perforin/CDC (MACPF/CDC) superfamily, containing pore formers responsible for controlling infectious disease and cancer in humans.
openaire   +2 more sources

In vitro reconstitution of substrate dislocation from the endoplasmic reticulum using Perfringolysin O

The FASEB Journal, 2011
Secretory proteins unable to assemble into their native states in the endoplasmic reticulum (ER) are transported back or “dislocated” into the cytosol for ER‐associated degradation (ERAD). To examine different roles of components in ERAD we have taken a biochemical approach to reconstitute the process of dislocation of misfolded ...
openaire   +1 more source

More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display. [PDF]

RSC Adv, 2020
Šakanović A, Kranjc N, Omersa N, Podobnik M, Anderluh G.   +4 more
europepmc   +1 more source

In vitro competition with Bifidobacterium strains impairs potentially pathogenic growth of Clostridium perfringens on 2′-fucosyllactose

Gut Microbes
Fortifying infant formula with human milk oligosaccharides, such as 2'-fucosyllactose (2'-FL), is a global trend. Previous studies have shown the inability of pathogenic gut microbes to utilize 2'-FL. However, the present study demonstrates that the type
Aruto Nakajima, Aleksandr A. Arzamasov, Mikiyasu Sakanaka, Ryuta Murakami, Tomoya Kozakai, Keisuke Yoshida, Toshihiko Katoh, Miriam N. Ojima, Junko Hirose, Saeko Nagao, Jin-Zhong Xiao, Toshitaka Odamaki, Dmitry A. Rodionov, Takane Katayama   +13 more
doaj   +1 more source

In vitro evolution driven by epistasis reveals alternative cholesterol-specific binding motifs of perfringolysin O. [PDF]

J Biol Chem
Šakanović A, Kranjc N, Omersa N, Aden S, Kežar A, Kisovec M, Zavec AB, Caserman S, Gilbert RJC, Podobnik M, Crnković A, Anderluh G.   +11 more
europepmc   +1 more source

Mechanistic Insights into the Cholesterol-dependent Binding of Perfringolysin O-based Probes and Cell Membranes. [PDF]

Sci Rep, 2017
Johnson BB, Breña M, Anguita J, Heuck AP.   +3 more
europepmc   +1 more source

Perfringolysin O structure and mechanism of pore formation as a paradigm for cholesterol-dependent cytolysins. [PDF]

Subcell Biochem, 2014
Johnson BB, Heuck AP.
europepmc   +1 more source

The influence of natural lipid asymmetry upon the conformation of a membrane-inserted protein (perfringolysin O). [PDF]

J Biol Chem, 2014
Lin Q, London E.
europepmc   +1 more source