Evidence map›Paper›PMID 26581778›Full record

ArticleProtein expression and purification2016

Simple method for purification of enterotoxigenic Escherichia coli fimbriae.

Brittany Curtis, Christen Grassel, Rachel S Laufer, Khandra T Sears, Marcela F Pasetti, Eileen M Barry, Raphael Simon

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

Article in Protein expression and purification, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 32% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

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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

7 authors at 1 institution in 1 country.

Brittany CurtisCenter for Vaccine Development, University of Maryland Medical School, Baltimore, MD, USA; Department of Medicine, University of Maryland Medical School, Baltimore, MD, USA.
Christen GrasselCenter for Vaccine Development, University of Maryland Medical School, Baltimore, MD, USA; Department of Medicine, University of Maryland Medical School, Baltimore, MD, USA.
Rachel S LauferCenter for Vaccine Development, University of Maryland Medical School, Baltimore, MD, USA; Department of Medicine, University of Maryland Medical School, Baltimore, MD, USA.
Khandra T SearsCenter for Vaccine Development, University of Maryland Medical School, Baltimore, MD, USA; Department of Pediatrics, University of Maryland Medical School, Baltimore, MD, USA.
Marcela F PasettiCenter for Vaccine Development, University of Maryland Medical School, Baltimore, MD, USA; Department of Pediatrics, University of Maryland Medical School, Baltimore, MD, USA.
Eileen M BarryCenter for Vaccine Development, University of Maryland Medical School, Baltimore, MD, USA; Department of Medicine, University of Maryland Medical School, Baltimore, MD, USA.
Raphael SimonCenter for Vaccine Development, University of Maryland Medical School, Baltimore, MD, USA; Department of Medicine, University of Maryland Medical School, Baltimore, MD, USA. Electronic address: rsimon@medicine.umaryland.edu.
University of Maryland, Baltimore · US

Funding

Shigella Live Vector-Based Multivalent VaccineU19AI109776 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI LEVINE, MYRON MAX · 2014 to 2018
$25.4M
NIAID NIH HHS U19 AI109776
6 · The paper itself

Abstract

Enterotoxigenic Escherichia coli (ETEC) are endemic pathogens in the developing world. They frequently cause illness in travelers, and are among the most prevalent causes of diarrheal disease in children. Pathogenic ETEC strains employ fimbriae as adhesion factors to bind the luminal surface of the intestinal epithelium and establish infection. Accordingly, there is marked interest in immunoprophylactic strategies targeting fimbriae to protect against ETEC infections. Multiple strategies have been reported for purification of ETEC fimbriae, however none is ideal. Purification has typically involved the use of highly virulent wild-type strains. We report here a simple and improved method to purify ETEC fimbriae, which was applied to obtain two different Class 5 fimbriae types of clinical relevance (CFA/I and CS4) expressed recombinantly in E. coli production strains. Following removal from cells by shearing, fimbriae proteins were purified by orthogonal purification steps employing ultracentrifugation, precipitation, and ion-exchange membrane chromatography. Purified fimbriae demonstrated the anticipated size and morphology by electron microscopy analysis, contained negligible levels of residual host cell proteins, nucleic acid, and endotoxin, and were recognized by convalescent human anti-sera.

Indexed as

Antibodies, BacterialChemical PrecipitationChromatography, GelChromatography, High Pressure LiquidChromatography, Ion ExchangeEnterotoxigenic Escherichia coliEscherichia coli ProteinsEscherichia coli VaccinesFimbriae, BacterialFimbriae ProteinsHumansImmunoglobulin GUltracentrifugationAntibodies, BacterialEscherichia coli ProteinsEscherichia coli VaccinesFimbriae ProteinsImmunoglobulin GEscherichia coliFimbriaePurification

Identifiers

PMID26581778
PMCPMC4721563
OpenAlexW2268593010

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.