English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Listeriolysin O (LLO) is a cholesterol-dependent cytolysin that mediates escape of  L. monocytogenes  from phagosomes and enables the bacteria to grow within the host. LLO is a versatile tool allowing  Listeria  to trigger several cellular responses. In this study, rapid phosphorylation of ERK1/2 on Caco-2 cells caused by  Listeria  infection was demonstrated to be highly dependent on LLO activity. The effect could be strongly induced by adding purified recombinant LLO alone and could be inhibited by exogenous cholesterol. Lack of the PEST sequence, known to tightly control cytotoxicity of LLO, did not affect ERK1/2 activation. However, the recombinant non-cytolytic LLO T515AL516A , with mutations in the cholesterol-binding motif, was unable to trigger this response. Recombinant LLO N478AV479A , which lacks most of the cytolytic activity, also failed to activate ERK1/2 phosphorylation, and this effect could be rescued when the protein concentration reached a cytolytic level. Infection with an LLO-deficient mutant (Δ hly ) or the mutant complementing LLO T515AL516A  abrogated the capacity of the bacteria to activate ERK1/2. However, infection with the Δ hly  mutant complementing LLO N478AV479A , which retained partial pore-forming ability and could grow intracellularly, was capable of triggering ERK1/2 phosphorylation. Collectively, these data suggest that ERK1/2 activation by  L. monocytogenes  depends on the permeabilization activity of LLO and more importantly correlates with the cholesterol-binding motif of LLO.

Listeriolysin O Pore-Forming Activity Is Required for ERK1/2 Phosphorylation During Listeria monocytogenes Infection