Evidence map›Paper›PMID 33007034›Full record

ArticlePLoS pathogens2020

Chaperone-tip adhesin complex is vital for synergistic activation of CFA/I fimbriae biogenesis.

Li-Hui He, Hao Wang, Yang Liu, Mei Kang, Tao Li, Chang-Cheng Li, Ai-Ping Tong, Yi-Bo Zhu, Ying-Jie Song, Stephen J Savarino and 3 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2020. 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
0.4field-weighted citation impact, top 37% 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. Article
  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

13 authors at 4 institutions in 2 countries.

Li-Hui HeCenter of Infectious Diseases, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Hao WangHenry M. Jackson Foundation for the Advancement of Military Medicine, Bethesda, MD, United States of America.ORCID 0000-0001-5173-8089
Yang LiuHenry M. Jackson Foundation for the Advancement of Military Medicine, Bethesda, MD, United States of America.
Mei KangDepartment of Laboratory medicine, West China Hospital, Sichuan University, Chengdu, China.
Tao LiCenter of Infectious Diseases, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Chang-Cheng LiCenter of Infectious Diseases, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Ai-Ping TongCenter of Infectious Diseases, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Yi-Bo ZhuCenter of Infectious Diseases, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Ying-Jie SongCenter of Infectious Diseases, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.
Stephen J SavarinoEnteric Diseases Department, Infectious Diseases Directorate, Naval Medical Research Center, Silver Spring, MD, United States of America.
Michael G ProutyEnteric Diseases Department, Infectious Diseases Directorate, Naval Medical Research Center, Silver Spring, MD, United States of America.
Di XiaLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, United States of America.
Rui BaoCenter of Infectious Diseases, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.ORCID 0000-0002-6083-8716
Sichuan University · CNHenry M. Jackson Foundation · USNaval Medical Research Command · USNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Colonization factor CFA/I defines the major adhesive fimbriae of enterotoxigenic Escherichia coli and mediates bacterial attachment to host intestinal epithelial cells. The CFA/I fimbria consists of a tip-localized minor adhesive subunit, CfaE, and thousands of copies of the major subunit CfaB polymerized into an ordered helical rod. Biosynthesis of CFA/I fimbriae requires the assistance of the periplasmic chaperone CfaA and outer membrane usher CfaC. Although the CfaE subunit is proposed to initiate the assembly of CFA/I fimbriae, how it performs this function remains elusive. Here, we report the establishment of an in vitro assay for CFA/I fimbria assembly and show that stabilized CfaA-CfaB and CfaA-CfaE binary complexes together with CfaC are sufficient to drive fimbria formation. The presence of both CfaA-CfaE and CfaC accelerates fimbria formation, while the absence of either component leads to linearized CfaB polymers in vitro. We further report the crystal structure of the stabilized CfaA-CfaE complex, revealing features unique for biogenesis of Class 5 fimbriae.

Indexed as

Adhesins, BacterialAmino Acid SequenceCytoplasmEnterotoxigenic Escherichia coliEscherichia coli ProteinsFimbriae, BacterialFimbriae ProteinsMolecular ChaperonesProtein ConformationSequence Homology, Amino AcidAdhesins, BacterialEscherichia coli ProteinsFimbriae ProteinsMolecular Chaperones

Identifiers

PMID33007034
PMCPMC7531860
OpenAlexW3034624361

What OpenQuestion holds

Textmetadata
LicenceCC0
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.