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

Structure-function analysis of the self-recognizing Antigen 43 autotransporter protein from Escherichia coli.

Molecular microbiology - 1 Jan 2004

Klemm Per, Hjerrild Louise, Gjermansen Morten, Schembri Mark A

Abstract excerpt

Antigen 43 (Ag43) is a self-recognizing surface adhesin found in most Escherichia coli strains. Expression of Ag43 confers aggregation and fluffing of cells, promotes biofilm formation and is associated with enhanced resistance to antimicrobial agents. Ag43 is an autotransporter protein and consists of two moieties: a transporter, the beta-module, and a passenger domain, the alpha-module. Here we have employed...

Read the complete abstract on PubMed

Topics

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

Share to Adhesins, Bacterial
Share to Adhesins, Escherichia coli

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Antigens, Bacterial

Share to Arabinose

Share to Bacterial Outer Membrane Proteins

Share to Biological Transport

Share to Protein Structure, Secondary

Share to Restriction Mapping

Source

Identifiers

PMID: 14651628
DOI: 10.1046/j.1365-2958.2003.03833.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure-function analysis of the self-recognizing Antigen 43 autotransporter protein from Escherichia coli.PMID 14651628Read ↗

Regulation and function of Ag43 (flu).Semantic proximity Read ↗

Extracellular loops of the β-barrel domain catalyze rapid folding for function of self-associating autotransportersSemantic proximity Read ↗

Revisiting the functions of periplasmic chaperones in the quality control of the autotransporter Ag43 using a phenotypically homogeneous Escherichia coli strain.Semantic proximity Read ↗

Functional Analysis of Antigen 43 in Uropathogenic<i>Escherichia coli</i>Reveals a Role in Long-Term Persistence in the Urinary TractSemantic proximity Read ↗

The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping.Semantic proximity Read ↗

Identification of antigen Ag43 in uropathogenic Escherichia coli Dr+ strains and defining its role in the pathogenesis of urinary tract infections.Semantic proximity Read ↗

Antigen 43, the major phase-variable protein of the Escherichia coli outer membrane, can exist as a family of proteins encoded by multiple alleles.Semantic proximity Read ↗

Antigen-43-mediated autoaggregation of Escherichia coli is blocked by fimbriation.Semantic proximity Read ↗

The outer membrane protein, antigen 43, mediates cell-to-cell interactions within Escherichia coli biofilms.Semantic proximity Read ↗

The dynamics and pH-dependence of Ag43 adhesins' self-association probed by atomic force spectroscopy.Semantic proximity Read ↗

Structure-function analysis of the TibA self-associating autotransporter reveals a modular organization.Semantic proximity Read ↗

Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment.Semantic proximity Read ↗

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