A bacterial encoded protein induces extreme multinucleation and cell-cell internalization in intestinal cells

Paul Dean, Brendan Kenny

Research output: Contribution to journalArticle

Abstract

Despite extensive study, the molecular mechanisms that lead to multinucleation and cell enlargement (hypertrophy) remain poorly understood. Here, we show that a single bacterial virulence protein, EspF, from the human pathogen enteropathogenic E. coli induces extreme multi-nucleation in small intestinal epithelial cells. Ectopic expression of EspF induced cell-cell internalization events, presumably responsible for the enlarged multinucleated cells. These extreme phenotypes were dependent on a C-terminal polyproline-rich domain in EspF and not linked to the targeting of mitochondria or the nucleolus. The subversive functions of EspF may provide valuable insight into the molecular mechanisms that mediate cell fusion, multinucleation and cell hypertrophy.
Original languageEnglish
Pages (from-to)e22639
JournalTissue Barriers
Volume1
Issue number1
DOIs
Publication statusPublished - 1 Jan 2013

Fingerprint

Mitochondria
Bacterial Proteins
Pathogens
Escherichia coli
Nucleation
Fusion reactions
Hypertrophy
Cell Enlargement
Enteropathogenic Escherichia coli
Cell Fusion
Virulence
Epithelial Cells
Phenotype
polyproline

Cite this

@article{6cab89f263734505a0e2bf47d5efa2f2,
title = "A bacterial encoded protein induces extreme multinucleation and cell-cell internalization in intestinal cells",
abstract = "Despite extensive study, the molecular mechanisms that lead to multinucleation and cell enlargement (hypertrophy) remain poorly understood. Here, we show that a single bacterial virulence protein, EspF, from the human pathogen enteropathogenic E. coli induces extreme multi-nucleation in small intestinal epithelial cells. Ectopic expression of EspF induced cell-cell internalization events, presumably responsible for the enlarged multinucleated cells. These extreme phenotypes were dependent on a C-terminal polyproline-rich domain in EspF and not linked to the targeting of mitochondria or the nucleolus. The subversive functions of EspF may provide valuable insight into the molecular mechanisms that mediate cell fusion, multinucleation and cell hypertrophy.",
author = "Paul Dean and Brendan Kenny",
year = "2013",
month = "1",
day = "1",
doi = "10.4161/tisb.22639",
language = "English",
volume = "1",
pages = "e22639",
journal = "Tissue Barriers",
issn = "2168-8362",
publisher = "Taylor and Francis Ltd.",
number = "1",

}

A bacterial encoded protein induces extreme multinucleation and cell-cell internalization in intestinal cells. / Dean, Paul; Kenny, Brendan.

In: Tissue Barriers, Vol. 1, No. 1, 01.01.2013, p. e22639.

Research output: Contribution to journalArticle

TY - JOUR

T1 - A bacterial encoded protein induces extreme multinucleation and cell-cell internalization in intestinal cells

AU - Dean, Paul

AU - Kenny, Brendan

PY - 2013/1/1

Y1 - 2013/1/1

N2 - Despite extensive study, the molecular mechanisms that lead to multinucleation and cell enlargement (hypertrophy) remain poorly understood. Here, we show that a single bacterial virulence protein, EspF, from the human pathogen enteropathogenic E. coli induces extreme multi-nucleation in small intestinal epithelial cells. Ectopic expression of EspF induced cell-cell internalization events, presumably responsible for the enlarged multinucleated cells. These extreme phenotypes were dependent on a C-terminal polyproline-rich domain in EspF and not linked to the targeting of mitochondria or the nucleolus. The subversive functions of EspF may provide valuable insight into the molecular mechanisms that mediate cell fusion, multinucleation and cell hypertrophy.

AB - Despite extensive study, the molecular mechanisms that lead to multinucleation and cell enlargement (hypertrophy) remain poorly understood. Here, we show that a single bacterial virulence protein, EspF, from the human pathogen enteropathogenic E. coli induces extreme multi-nucleation in small intestinal epithelial cells. Ectopic expression of EspF induced cell-cell internalization events, presumably responsible for the enlarged multinucleated cells. These extreme phenotypes were dependent on a C-terminal polyproline-rich domain in EspF and not linked to the targeting of mitochondria or the nucleolus. The subversive functions of EspF may provide valuable insight into the molecular mechanisms that mediate cell fusion, multinucleation and cell hypertrophy.

U2 - 10.4161/tisb.22639

DO - 10.4161/tisb.22639

M3 - Article

VL - 1

SP - e22639

JO - Tissue Barriers

JF - Tissue Barriers

SN - 2168-8362

IS - 1

ER -