Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Shigella applies molecular mimicry to subvert vinculin and invade host cells.

The Journal of cell biology - 6 Nov 2006

Izard Tina, Tran Van Nhieu Guy, Bois Philippe R J

Abstract excerpt

Shigella flexneri, the causative agent of bacillary dysentery, injects invasin proteins through a type III secretion apparatus upon contacting the host cell, which triggers pathogen internalization. The invasin IpaA is essential for S. flexneri pathogenesis and binds to the cytoskeletal protein vinculin to facilitate host cell entry. We report that IpaA harbors two vinculin-binding sites (VBSs) within its...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Caco-2 Cells
Share to Crystallization
Share to Cytoskeleton

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dysentery, Bacillary

Share to Molecular Mimicry

Share to Shigella flexneri

Share to Vinculin

Source

Open in PubMed Open full text

Identifiers

PMID: 17088427
DOI: 10.1083/jcb.200605091
PMCID: PMC2064523

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Shigella applies molecular mimicry to subvert vinculin and invade host cells.PMID 17088427Read ↗

IpaA reveals distinct modes of vinculin activation during Shigella invasion and cell-matrix adhesion.Semantic proximity Read ↗

IpaA targets beta1 integrins and rho to promote actin cytoskeleton rearrangements necessary for Shigella entry.Semantic proximity Read ↗

Shigella hijacks the exocyst to cluster macropinosomes for efficient vacuolar escapeSemantic proximity Read ↗

Uncivil Engineers: Chlamydia , Salmonella and Shigella Alter Cytoskeleton Architecture to Invade Epithelial CellsSemantic proximity Read ↗

Activation of Shigella flexneri type 3 secretion requires a host-induced conformational change to the translocon poreSemantic proximity Read ↗

A translocation-competent pore is required for <i>Shigella flexneri</i> to escape from the double membrane vacuole during intercellular spreadSemantic proximity Read ↗

A system for identifying post-invasion functions of invasion genes: requirements for the Mxi-Spa type III secretion pathway of Shigella flexneri in intercellular dissemination.Semantic proximity Read ↗

Pathogenesis of shigellosis: from molecular and cellular biology of epithelial cell invasion to tissue inflammation and vaccine development.Semantic proximity Read ↗

<i>Shigella flexneri</i> disruption of host cell-cell tension promotes intercellular spreadSemantic proximity Read ↗

Actin-based motility is sufficient for bacterial membrane protrusion formation and host cell uptake.Semantic proximity Read ↗

Pushing boundaries: mechanisms enabling bacterial pathogens to spread between cellsSemantic proximity Read ↗

Pathogenic microbes manipulate cofilin activity to subvert actin cytoskeletonSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.