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

The S-layer proteins of Tannerella forsythia are secreted via a type IX secretion system that is decoupled from protein O-glycosylation.

Molecular oral microbiology - 1 Dec 2014

Tomek M B, Neumann L, Nimeth I, Koerdt A, Andesner P, Messner P, Mach L, Potempa J S, Schäffer C

Abstract excerpt

Conserved C-terminal domains (CTD) have been shown to act as a signal for the translocation of certain proteins across the outer membrane of Bacteroidetes via a type IX secretion system (T9SS). The genome sequence of the periodontal pathogen Tannerella forsythia predicts the presence of the components for a T9SS in conjunction with a suite of CTD proteins. T. forsythia is covered with a two-dimensional...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Secretion Systems
Share to Bacteroidetes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Biofilms

Share to Gene Knockout Techniques

Share to Glycosylation

Share to Microscopy, Electron, Scanning

Share to Microscopy, Electron, Transmission

Share to Spectrometry, Mass, Electrospray Ionization

Source

Open in PubMed Open full text

Identifiers

PMID: 24943676
DOI: 10.1111/omi.12062
PMCID: PMC4232474

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

The S-layer proteins of Tannerella forsythia are secreted via a type IX secretion system that is decoupled from protein O-glycosylation.PMID 24943676Read ↗

Lack of a surface layer in Tannerella forsythia mutants deficient in the type IX secretion system.Semantic proximity Read ↗

Analysis of the cell surface layer ultrastructure of the oral pathogen Tannerella forsythiaSemantic proximity Read ↗

The intriguing strategies of Tannerella forsythia's host interactionSemantic proximity Read ↗

A bacterial glycan core linked to surface (S)-layer proteins modulates host immunity through Th17 suppression.Semantic proximity Read ↗

Structural and functional probing of PorZ, an essential bacterial surface component of the type-IX secretion system of human oral-microbiomic Porphyromonas gingivalis.Semantic proximity Read ↗

Potential of the Tannerella forsythia S-layer to delay the immune response.Semantic proximity Read ↗

Immune response profiling of primary monocytes and oral keratinocytes to different Tannerella forsythia strains and their cell surface mutants.Semantic proximity Read ↗

The Type IX Secretion System (T9SS): Highlights and Recent Insights into Its Structure and FunctionSemantic proximity Read ↗

A pseudaminic acid or a legionaminic acid derivative transferase is strain-specifically implicated in the general protein O-glycosylation system of the periodontal pathogen Tannerella forsythia.Semantic proximity Read ↗

Glycosylation orchestrates virulence and pathogenicity of periodontal keystone pathogensSemantic proximity Read ↗

Role of a Tannerella forsythia exopolysaccharide synthesis operon in biofilm development.Semantic proximity Read ↗

Genetic Characteristics and Pathogenic Mechanisms of Periodontal PathogensSemantic proximity Read ↗

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