Evidence map›Paper›PMID 27627030›Full record

ArticleMolecular microbiology2016

Off-pathway assembly of fimbria subunits is prevented by chaperone CfaA of CFA/I fimbriae from enterotoxigenic E. coli.

Rui Bao, Yang Liu, Stephen J Savarino, Di Xia

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.2field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. EnterotoxigenicProceedings of the National Academy of Sciences of the United States of America · 2018
    Trial
  2. Article
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 4 institutions in 2 countries.

Rui BaoDivision of Infectious Diseases, National Key Laboratory of Biotherapy/Collaborative Innovation Center of Biotherapy, West China Hospitals, Sichuan University, Chengdu, 610041, China.
Yang LiuEnteric Diseases Department, Infectious Diseases Directorate, Naval Medical Research Center, Silver Spring, MD, 20910-7500, USA.
Stephen J SavarinoEnteric Diseases Department, Infectious Diseases Directorate, Naval Medical Research Center, Silver Spring, MD, 20910-7500, USA.
Di XiaLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD, 20892, USA.
Center for Cancer Research · USNational Cancer Institute · USNaval Medical Research Command · USUniformed Services University of the Health Sciences · US

Funding

Structural studies of fimbriae of enterotoxigenic E. coli (ETEC)ZIABC010735 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI XIA, DI S · 2009 to 2017
$1.2M
Structural studies of fimbriae of enterotoxigenic E. coli (ETEC)Z01BC010735 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI XIA, DI S · 2007 to 2008
$225k
Intramural NIH HHS Z01 BC010735Intramural NIH HHS Z99 CA999999Intramural NIH HHS ZIA BC010735
6 · The paper itself

Abstract

The assembly of the class 5 colonization factor antigen I (CFA/I) fimbriae of enterotoxigenic E. coli was proposed to proceed via the alternate chaperone-usher pathway. Here, we show that in the absence of the chaperone CfaA, CfaB, the major pilin subunit of CFA/I fimbriae, is able to spontaneously refold and polymerize into cyclic trimers. CfaA kinetically traps CfaB to form a metastable complex that can be stabilized by mutations. Crystal structure of the stabilized complex reveals distinctive interactions provided by CfaA to trap CfaB in an assembly competent state through donor-strand complementation (DSC) and cleft-mediated anchorage. Mutagenesis indicated that DSC controls the stability of the chaperone-subunit complex and the cleft-mediated anchorage of the subunit C-terminus additionally assist in subunit refolding. Surprisingly, over-stabilization of the chaperone-subunit complex led to delayed fimbria assembly, whereas destabilizing the complex resulted in no fimbriation. Thus, CfaA acts predominantly as a kinetic trap by stabilizing subunit to avoid its off-pathway self-polymerization that results in energetically favorable trimers and could serve as a driving force for CFA/I pilus assembly, representing an energetic landscape unique to class 5 fimbria assembly.

Indexed as

Amino Acid MotifsEnterotoxigenic Escherichia coliEscherichia coliEscherichia coli ProteinsFimbriae, BacterialFimbriae ProteinsMolecular ChaperonesProtein Structure, TertiaryProtein SubunitsStructure-Activity Relationshipcolonization factor antigensEscherichia coli ProteinsFimbriae ProteinsMolecular ChaperonesProtein Subunits

Identifiers

PMID27627030
PMCPMC5161713
OpenAlexW2521212801

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.