Evidence map›Paper›PMID 32147470›Full record

ArticleActa biomaterialia2020

Antibody-mediated trapping in biological hydrogels is governed by sugar-sugar hydrogen bonds.

Jennifer L Schiller, Mary M Fogle, Olivia Bussey, William J Kissner, David B Hill, Samuel K Lai

Open access · bronzeAbstract read
In one paragraph

Article in Acta biomaterialia, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Tethering of soluble immune effectors to mucin and chitin reflects a convergent and dynamic role in gut immunity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  2. Recombinant neutralizing secretory IgA antibodies for preventing mucosal acquisition and transmission of SARS-CoV-2.Molecular therapy : the journal of the American Society of Gene Therapy · 2024
    Article
  3. Article
  4. Review
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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

6 authors at 1 institution in 1 country.

Jennifer L SchillerDivision of Pharmacoengineering and Molecular Pharmaceutics, Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Mary M FogleDivision of Pharmacoengineering and Molecular Pharmaceutics, Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Olivia BusseyDivision of Pharmacoengineering and Molecular Pharmaceutics, Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
William J KissnerDepartment of Physics and Astronomy, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
David B HillDepartment of Physics and Astronomy, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Marsico Lung Institute/CF Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Samuel K LaiDivision of Pharmacoengineering and Molecular Pharmaceutics, Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; UNC/NCSU Joint Department of Biomedical Engineering, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Department of Microbiology & Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. Electronic address: lai@unc.edu.
University of North Carolina at Chapel Hill · US

Funding

Overcoming anti-PEG immunity to restore prolonged circulation and efficacy of PEGylated therapeuticsR01HL141934 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LAI, SAMUEL, ZAMBONI, WILLIAM C · 2018 to 2021
$2.7M
NHLBI NIH HHS R01 HL141934
6 · The paper itself

Abstract

N-glycans on IgG and IgM antibodies (Ab) facilitate Ab-mediated crosslinking of viruses and nanoparticles to the major structural elements of mucus and basement membranes. Nevertheless, the chemical moieties in these biological hydrogel matrices to which Ab can bind remain poorly understood. To gain insights into the chemistries that support Ab-matrix interactions, we systematically evaluated IgG- and IgM-mediated trapping of nanoparticles in different polysaccharide-based biogels with unique chemical features. In agarose, composed of alternating d-galactose and 3,6-anhydro-l-galactopyranose (i.e. hydroxyl groups only), anti-PEG IgM but not anti-PEG IgG trapped PEGylated nanoparticles. In alginate, comprised of homopolymeric blocks of mannuronate and guluronate (i.e. both hydroxyl and carboxyl groups), both IgG and IgM trapped PEGylated nanoparticles. In contrast, chitosan, comprised primarily of glucosamine (i.e. both hydroxyl and primary amine groups), did not facilitate either IgG- or IgM-mediated trapping. IgG-mediated trapping in alginate was abrogated upon removal of IgG N-glycans, whereas IgM-mediated trapping was eliminated in agarose but not alginate upon desialylation. These results led us to propose a model in which hydrogen bonding between carboxyl and hydroxyl groups of glycans on both Ab and matrix facilitates Ab-mediated trapping of pathogens in biogels. Our work here offers a blueprint for designing de novo hydrogels that could harness Ab-matrix interactions for various biomedical and biological applications. STATEMENT OF SIGNIFICANCE: Here, we interrogated the molecular mechanism of antibody-mediated trapping to address what are the chemical moieties on biogels that are essential for facilitating trapping in biogels. We systematically evaluated the potencies of IgG and IgM to trap nanoparticles in different polysaccharide-based biogels with unique and highly defined chemical moieties: hydroxyl groups (agarose), amine groups (chitosan), and carboxyl groups (alginate). We discovered that only hydroxyl/carboxyl hydrogen bonds (and stronger) are sufficiently strong enough to facilitate antibody-mediated trapping; weaker hydroxyl/hydroxyl bonds or hydroxyl/amine bonds fail to adequately slow particles. Our findings presents the first blueprint for how to engineer de novo biogels that are capable of harnessing antibodies to immobilize foreign entities in the biogels, for applications ranging from infectious disease to contraception to purification processes.

Indexed as

AlginatesChitosanHydrogelsHydrogen BondingImmunoglobulin GImmunoglobulin MNanoparticlesPolyethylene GlycolsPolystyrenesProtein BindingSepharoseAlginatesChitosanHydrogelsImmunoglobulin GImmunoglobulin Mmethoxy polyethylene glycol aminePolyethylene GlycolsPolystyrenesSepharoseAntibodiesBiological hydrogelsGlycosylationHydrogen bonds

Identifiers

PMID32147470
PMCPMC8812814
OpenAlexW3012067211

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.