Evidence map›Paper›PMID 37649182›Full record

ArticleSmall (Weinheim an der Bergstrasse, Germany)2023

Multivalent Targeting of the Asialoglycoprotein Receptor by Virus-Like Particles.

Robert Hincapie, Sonia Bhattacharya, Michael M Baksh, Carlos A Sanhueza, Elisa Schrader Echeverri, Hyejin Kim, Kalina Paunovska, Ananda R Podilapu, Minghao Xu, James E Dahlman and 1 more

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

Article in Small (Weinheim an der Bergstrasse, Germany), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

9 citing papers in PubMed, 13 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

11 authors at 1 institution in 1 country.

Robert HincapieSchool of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive, Atlanta, GA, 30332, USA.
Sonia BhattacharyaSchool of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive, Atlanta, GA, 30332, USA.
Michael M BakshSchool of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive, Atlanta, GA, 30332, USA.
Carlos A SanhuezaSchool of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive, Atlanta, GA, 30332, USA.
Elisa Schrader EcheverriWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory School of Medicine, 313 Ferst Dr NW, Atlanta, GA, 30332, USA.
Hyejin KimWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory School of Medicine, 313 Ferst Dr NW, Atlanta, GA, 30332, USA.
Kalina PaunovskaWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory School of Medicine, 313 Ferst Dr NW, Atlanta, GA, 30332, USA.
Ananda R PodilapuSchool of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive, Atlanta, GA, 30332, USA.
Minghao XuSchool of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive, Atlanta, GA, 30332, USA.
James E DahlmanWallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology and Emory School of Medicine, 313 Ferst Dr NW, Atlanta, GA, 30332, USA.
M G FinnSchool of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive, Atlanta, GA, 30332, USA.ORCID 0000-0001-8247-3108
Georgia Institute of Technology · US

Funding

Development of the Next Generation of Conjugate VaccinesR01AI139748 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI TEYTON, LUC · 2018 to 2021
$3.4M
NIAID NIH HHS R01 AI139748
6 · The paper itself

Abstract

The asialoglycoprotein receptor (ASGPR) is expressed in high density on hepatocytes. Multivalent variants of galactosyl carbohydrates bind ASGPR with high affinity, enabling hepatic delivery of ligand-bound cargo. Virus-like particle (VLP) conjugates of a relatively high-affinity ligand were efficiently endocytosed by ASGPR-expressing cells in a manner strongly dependent on the nature and density of ligand display, with the best formulation using a nanomolar-, but not a picomolar-level, binder. Optimized particles were taken up by HepG2 cells with greater efficiency than competing small molecules or the natural multigalactosylated ligand, asialoorosomucoid. Upon systemic injection in mice, these VLPs were rapidly cleared to the liver and were found in association with sinusoidal endothelial cells, Kupffer cells, hepatocytes, dendritic cells, and other immune cells. Both ASGPR-targeted and nontargeted particles were distributed similarly to endothelial and Kupffer cells, but targeted particles were distributed to a greater number and fraction of hepatocytes. Thus, selective cellular trafficking in the liver is difficult to achieve: even with the most potent ASGPR targeting available, barrier cells take up much of the injected particles and hepatocytes are accessed only approximately twice as efficiently in the best case.

Indexed as

Endothelial CellsLiverAnimalsAsialoglycoprotein ReceptorHepatocytesLigandsMiceAsialoglycoprotein ReceptorLigandshepatocellular targetingnanoparticlesprotein-carbohydrate conjugatesvirus-like particles

Identifiers

PMID37649182
PMCPMC10840735
OpenAlexW4386306187

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.