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

Functional Role of N- and C-Terminal Amino Acids in the Structural Subunits of Colonization Factor CS6 Expressed by Enterotoxigenic Escherichia coli.

Journal of bacteriology - 1 May 2016

Debnath Anusuya, Sabui Subrata, Wajima Takeaki, Hamabata Takashi, Banerjee Rajat, Chatterjee Nabendu Sekhar

Abstract excerpt

UNLABELLED: CS6 is a common colonization factor expressed by enterotoxigenic Escherichia coli It is a two-subunit protein consisting of CssA and CssB in an equal stoichiometry, assembled via the chaperone-usher pathway into an afimbrial, oligomeric assembly on the bacterial cell surface. A recent structural study has predicted the involvement of the N- and C-terminal regions of the CS6 subunits in its assembly....

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Antigens, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Bacterial Adhesion

Share to Caco-2 Cells

Share to Enterotoxigenic Escherichia coli

Share to Escherichia coli Proteins

Share to Molecular Chaperones

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 26929298
DOI: 10.1128/JB.00657-15
PMCID: PMC4836235

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

Functional Role of N- and C-Terminal Amino Acids in the Structural Subunits of Colonization Factor CS6 Expressed by Enterotoxigenic Escherichia coli.PMID 26929298Read ↗

Role of different genes in the CS6 operon for surface expression of Enterotoxigenic Escherichia coli colonization factor CS6.Semantic proximity Read ↗

Mutations in the periplasmic chaperone leading to loss of surface expression of the colonization factor CS6 in enterotoxigenic Escherichia coli (ETEC) clinical isolates.Semantic proximity Read ↗

Allelic variation in colonization factor CS6 of enterotoxigenic Escherichia coli isolated from patients with acute diarrhoea and controls.Semantic proximity Read ↗

Two specific amino acid variations in colonization factor CS6 subtypes of enterotoxigenic Escherichia coli results in differential binding and pathogenicity.Semantic proximity Read ↗

Secretion of curli fibre subunits is mediated by the outer membrane-localized CsgG protein.Semantic proximity Read ↗

Identification and characterization of the novel colonization factor CS30 based on whole genome sequencing in enterotoxigenic Escherichia coli (ETEC).Semantic proximity Read ↗

Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificitySemantic proximity Read ↗

Structure and function of enterotoxigenic E scherichia coli fimbriae from differing assembly pathwaysSemantic proximity Read ↗

Structural and functional characterization of the Curli adaptor protein CsgFSemantic proximity Read ↗

Evolutionary and functional relationships of colonization factor antigen i and other class 5 adhesive fimbriae of enterotoxigenic Escherichia coli.Semantic proximity Read ↗

Constraints on lateral gene transfer in promoting fimbrial usher protein diversity and function.Semantic proximity Read ↗

Chaperone-usher pathways: diversity and pilus assembly mechanism.Semantic proximity Read ↗

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