Evidence map›Paper›PMID 20133740›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Delivery of foreign antigens by engineered outer membrane vesicle vaccines.

David J Chen, Nikolaus Osterrieder, Stephan M Metzger, Elizabeth Buckles, Anne M Doody, Matthew P DeLisa, David Putnam

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

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 158 papers.

0numbers the graph read from it
0cells of the map it votes in
158citing papers in PubMed
8.5field-weighted citation impact, top 2% 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

158 citing papers in PubMed, 301 citations in OpenAlex.

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  19. Genetically surface-modifiedBiotechnology reports (Amsterdam, Netherlands) · 2024
    Article
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98 more citing papers are in PubMed but not listed here.

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 2 countries.

David J ChenSchool of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY 14853, USA.
Nikolaus Osterrieder
Stephan M Metzger
Elizabeth Buckles
Anne M Doody
Matthew P DeLisa
David Putnam
Cornell University · US

Funding

Engineered Outer Membrane Vesicles as DNA Vaccine Delivery VehiclesR21EB005669 · NIBIB · CORNELL UNIVERSITY · PI PUTNAM, DAVID A · 2006 to 2007
$398k
NIBIB NIH HHS R21 EB005669NIBIB NIH HHS R21EB005669-01
6 · The paper itself

Abstract

As new disease threats arise and existing pathogens grow resistant to conventional interventions, attention increasingly focuses on the development of vaccines to induce protective immune responses. Given their admirable safety records, protein subunit vaccines are attractive for widespread immunization, but their disadvantages include poor immunogenicity and expensive manufacture. We show here that engineered Escherichia coli outer membrane vesicles (OMVs) are an easily purified vaccine-delivery system capable of greatly enhancing the immunogenicity of a low-immunogenicity protein antigen without added adjuvants. Using green-fluorescent protein (GFP) as the model subunit antigen, genetic fusion of GFP with the bacterial hemolysin ClyA resulted in a chimeric protein that elicited strong anti-GFP antibody titers in immunized mice, whereas immunization with GFP alone did not elicit such titers. Harnessing the specific secretion of ClyA to OMVs, the ClyA-GFP fusion was found localized in OMVs, resulting in engineered recombinant OMVs. The anti-GFP humoral response in mice immunized with the engineered OMV formulations was indistinguishable from the response to the purified ClyA-GFP fusion protein alone and equal to purified proteins absorbed to aluminum hydroxide, a standard adjuvant. In a major improvement over current practice, engineered OMVs containing ClyA-GFP were easily isolated by ultracentrifugation, effectively eliminating the need for laborious antigen purification from cell-culture expression systems. With the diverse collection of heterologous proteins that can be functionally localized with OMVs when fused with ClyA, this work signals the possibility of OMVs as a robust and tunable technology platform for a new generation of prophylactic and therapeutic vaccines.

Indexed as

AnimalsAntigensDrug Delivery SystemsEnzyme-Linked Immunosorbent AssayEscherichia coliEscherichia coli ProteinsGreen Fluorescent ProteinsHemolysin ProteinsMiceMicroscopy, Electron, TransmissionMicroscopy, FluorescenceProtein EngineeringTransport VesiclesUltracentrifugationVaccinesAntigensEscherichia coli ProteinsGreen Fluorescent ProteinsHemolysin ProteinshlyE protein, E coliVaccines

Identifiers

PMID20133740
PMCPMC2840271
OpenAlexW2050259218

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.