Evidence map›Paper›PMID 19206245›Full record

ArticleACS nano2009

Targeting vault nanoparticles to specific cell surface receptors.

Valerie A Kickhoefer, Muri Han, Sujna Raval-Fernandes, Michael J Poderycki, Raymond J Moniz, Dana Vaccari, Mariena Silvestry, Phoebe L Stewart, Kathleen A Kelly, Leonard H Rome

Abstract read
In one paragraph

Article in ACS nano, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
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

53 citing papers in PubMed.

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  14. International journal of molecular sciences · 2022
    Article
  15. The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design.International journal of molecular sciences · 2021
    Review
  16. Review
  17. 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

10 authors.

Valerie A KickhoeferDepartment of Biological Chemistry, David Geffen School of Medicine at UCLA, Los Angeles, California 90095-1737, USA.
Muri Han
Sujna Raval-Fernandes
Michael J Poderycki
Raymond J Moniz
Dana Vaccari
Mariena Silvestry
Phoebe L Stewart
Kathleen A Kelly
Leonard H Rome

Funding

MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
T-CELL MEDIATED IMMUNITY IN CHLAMYDIAL GENITAL INFECTIONR01AI026328 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KELLY, KATHLEEN A. · 1988 to 2012
$3.6M
Vaults as Nonviral Nucleic Acid Delivery VehiclesR01EB004553 · NIBIB · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ROME, LEONARD H · 2005 to 2008
$1.3M
T-Cell Mediated Immunity In Chlamydial Genital InfectionR21AI026328 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KELLY, KATHLEEN A. · 2001 to 2001
$298k
NIAID NIH HHS AI-026328NIAID NIH HHS R01 AI026328NIAID NIH HHS R21 AI026328NIBIB NIH HHS EB-004553NIBIB NIH HHS R01 EB004553NIGMS NIH HHS T32 GM008320NIGMS NIH HHS T32-GM008320
6 · The paper itself

Abstract

As a naturally occurring nanocapsule abundantly expressed in nearly all-eukaryotic cells, the barrel-shaped vault particle is perhaps an ideal structure to engineer for targeting to specific cell types. Recombinant vault particles self-assemble from 96 copies of the major vault protein (MVP), have dimensions of 72.5 x 41 nm, and have a hollow interior large enough to encapsulate hundreds of proteins. In this study, three different tags were engineered onto the C-terminus of MVP: an 11 amino acid epitope tag, a 33 amino acid IgG-binding peptide, and the 55 amino acid epidermal growth factor (EGF). These modified vaults were produced using a baculovirus expression system. Our studies demonstrate that recombinant vaults assembled from MVPs containing C-terminal peptide extensions display these tags at the top and bottom of the vault on the outside of the particle and can be used to specifically bind the modified vaults to epithelial cancer cells (A431) via the epidermal growth factor receptor (EGFR), either directly (EGF modified vaults) or as mediated by a monoclonal antibody (anti-EGFR) bound to recombinant vaults containing the IgG-binding peptide. The ability to target vaults to specific cells represents an essential advance toward using recombinant vaults as delivery vehicles.

Indexed as

AnimalsBinding SitesCell Line, TumorCell MembraneDendritic CellsEpitopesErbB ReceptorsHeLa CellsHumansImmunoglobulin GMiceNanoparticlesProtein BindingProtein Structure, TertiaryReceptors, Cell SurfaceEpitopesErbB ReceptorsImmunoglobulin GReceptors, Cell Surface

Identifiers

PMID19206245
PMCPMC2641028

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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.