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

Contribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri.

Journal of bacteriology - 1 Feb 2009

Wagner Jennifer K, Heindl Jason E, Gray Andrew N, Jain Sumita, Goldberg Marcia B

Abstract excerpt

IcsA is an outer membrane protein in the autotransporter family that is required for Shigella flexneri pathogenesis. Following its secretion through the Sec translocon, IcsA is incorporated into the outer membrane in a process that depends on YaeT, a component of an outer membrane beta-barrel insertion machinery. We investigated the role of the periplasmic chaperone Skp in IcsA maturation. Skp is required for the...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Blotting, Western

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA-Binding Proteins

Share to Immunoblotting

Share to Models, Biological

Share to Periplasm

Share to Protein Folding

Share to Shigella flexneri

Source

Open in PubMed Open full text

Identifiers

PMID: 19047350
DOI: 10.1128/JB.00989-08
PMCID: PMC2632083

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

Contribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri.PMID 19047350Read ↗

IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA.Semantic proximity Read ↗

IcsA, a polarly localized autotransporter with an atypical signal peptide, uses the Sec apparatus for secretion, although the Sec apparatus is circumferentially distributed.Semantic proximity Read ↗

Absence of O antigen suppresses Shigella flexneri IcsA autochaperone region mutations.Semantic proximity Read ↗

Disruption of IcsP, the major Shigella protease that cleaves IcsA, accelerates actin-based motility.Semantic 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 Genome-Scale Proteomic Screen Identifies a Role for DnaK in Chaperoning of Polar Autotransporters in<i>Shigella</i>Semantic proximity Read ↗

The SPI2-encoded SseA chaperone has discrete domains required for SseB stabilization and export, and binds within the C-terminus of SseB and SseD.Semantic proximity Read ↗

Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae.Semantic proximity Read ↗

Requirement for YaeT in the outer membrane assembly of autotransporter proteins.Semantic proximity Read ↗

Shigella flexneri cell-to-cell spread, and growth and inflammation in mice, is limited by the outer membrane protease IcsP.Semantic proximity Read ↗

Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins.Semantic proximity Read ↗

MxiA, MxiC and IpaD Regulate Substrate Selection and Secretion Mode in the T3SS of Shigella flexneri.Semantic proximity Read ↗

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