Evidence map›Paper›PMID 19515814›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Structure of CFA/I fimbriae from enterotoxigenic Escherichia coli.

Yong-Fu Li, Steven Poole, Kazuya Nishio, Ken Jang, Fatima Rasulova, Annette McVeigh, Stephen J Savarino, Di Xia, Esther Bullitt

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

60 citing papers in PubMed, 93 citations in OpenAlex.

  1. EnterotoxigenicProceedings of the National Academy of Sciences of the United States of America · 2018
    Trial
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  9. Comparative Pathogenomics ofInfection and immunity · 2021
    Article
  10. Impact of an alpha helix and a cysteine-cysteine disulfide bond on the resistance of bacterial adhesion pili to stress.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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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

9 authors at 5 institutions in 1 country.

Yong-Fu LiLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892-4256, USA.
Steven Poole
Kazuya Nishio
Ken Jang
Fatima Rasulova
Annette McVeigh
Stephen J Savarino
Di Xia
Esther Bullitt
Naval Medical Research Command · USBoston University · USCenter for Cancer Research · USNational Cancer Institute · USNational Institutes of Health · US

Funding

STRUCTURE/FUNCTION OF BACTERIAL ADHESION PILIR01GM055722 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI BULLITT, ESTHER · 1998 to 2009
$2.1M
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
NIGMS NIH HHS GM055722NIGMS NIH HHS R01 GM055722
6 · The paper itself

Abstract

Adhesion pili (fimbriae) play a critical role in initiating the events that lead to intestinal colonization and diarrheal disease by enterotoxigenic Escherichia coli (ETEC), an E. coli pathotype that inflicts an enormous global disease burden. We elucidate atomic structures of an ETEC major pilin subunit, CfaB, from colonization factor antigen I (CFA/I) fimbriae. These data are used to construct models for 2 morphological forms of CFA/I fimbriae that are both observed in vivo: the helical filament into which it is typically assembled, and an extended, unwound conformation. Modeling and corroborative mutational data indicate that proline isomerization is involved in the conversion between these helical and extended forms. Our findings affirm the strong structural similarities seen between class 5 fimbriae (from bacteria primarily causing gastrointestinal disease) and class 1 pili (from bacteria that cause urinary, respiratory, and other infections) in the absence of significant primary sequence similarity. They also suggest that morphological and biochemical differences between fimbrial types, regardless of class, provide structural specialization that facilitates survival of each bacterial pathotype in its preferred host microenvironment. Last, we present structural evidence for bacterial use of antigenic variation to evade host immune responses, in that residues occupying the predicted surface-exposed face of CfaB and related class 5 pilins show much higher genetic sequence variability than the remainder of the pilin protein.

Indexed as

Antigens, BacterialBinding SitesCrystallography, X-RayEnterotoxigenic Escherichia coliEscherichia coli InfectionsEscherichia coli ProteinsFimbriae ProteinsModels, MolecularMutationProlineProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsAntigens, Bacterialcolonization factor antigensEscherichia coli ProteinsFimbriae ProteinsProlineProtein Subunits

Identifiers

PMID19515814
PMCPMC2705562
OpenAlexW1991251012

What OpenQuestion holds

Textmetadata
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.