Logo image
Membrane permeabilization by Listeria monocytogenes phosphatidylinositol-specific phospholipase C is independent of phospholipid hydrolysis and cooperative with listeriolysin O
Journal article   Open access

Membrane permeabilization by Listeria monocytogenes phosphatidylinositol-specific phospholipase C is independent of phospholipid hydrolysis and cooperative with listeriolysin O

Howard Goldfine, Christopher Knob, Dennis Alford and Joe Bentz
Proceedings of the National Academy of Sciences - PNAS, v 92(7), pp 2979-2983
28 Mar 1995
PMID: 7708759
url
https://doi.org/10.1073/pnas.92.7.2979View
Published, Version of Record (VoR)Maybe Open Access (Publisher Bronze) Open

Abstract

Biotechnology Genes Infections Lipids Membranes Permeability
Potential cooperative interactions of Listeria monocytogenes phosphatidylinositol-specific phospholipase C (PI-PLC) and listeriolysin O (LLO) were examined in a liposome lysis assay. The data support a postulated accessory role for PI-PLC with LLO in lysing the primary phagosome of a macrophage.

Metrics

Details

UN Sustainable Development Goals (SDGs)

This publication has contributed to the advancement of the following goals:

#3 Good Health and Well-Being

InCites Highlights

Data related to this publication, from InCites Benchmarking & Analytics tool:

Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Logo image