Evidence map›Paper›PMID 30911061›Full record

ArticleScientific reports2019

Generation of a Fully Human scFv that binds Tumor-Specific Glycoforms.

Zhongpeng Lu, Kalika Kamat, Blake P Johnson, Catherin C Yin, Nathalie Scholler, Karen L Abbott

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. 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 14% 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, 18 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

6 authors at 3 institutions in 1 country.

Zhongpeng LuUniversity of Arkansas for Medical Sciences, Department of Biochemistry and Molecular Biology, Little Rock, AR, 72205, USA.
Kalika KamatSRI International Biosciences Division, Center for Cancer and Metabolism, Menlo Park, CA, 94025-3493, USA.
Blake P JohnsonOuachita Baptist University, Department of Biology, Arkadelphia, AR, 71998, USA.
Catherin C YinSRI International Biosciences Division, Center for Cancer and Metabolism, Menlo Park, CA, 94025-3493, USA.
Nathalie SchollerSRI International Biosciences Division, Center for Cancer and Metabolism, Menlo Park, CA, 94025-3493, USA.ORCID http://orcid.org/0000-0003-3743-7102
Karen L AbbottUniversity of Arkansas for Medical Sciences, Department of Biochemistry and Molecular Biology, Little Rock, AR, 72205, USA. kabbott@uams.edu.
SRI International · USUniversity of Arkansas for Medical Sciences · USOuachita Baptist University · US

Funding

Glycomics Laboratory for the Development of Ovarian Cancer BiomarkersU01CA226055 · NCI · UNIV OF ARKANSAS FOR MED SCIS · PI ABBOTT, KAREN L. · 2018 to 2022
$3.3M
Glycomics Laboratory for the Early Detection of Epithelial Ovarian CancerU01CA168870 · NCI · UNIV OF ARKANSAS FOR MED SCIS · PI ABBOTT, KAREN L. · 2012 to 2016
$2.0M
Novel Platform linking cancer-specific glycosylation with cell signaling outcomesR21CA229044 · NCI · UNIV OF ARKANSAS FOR MED SCIS · PI ABBOTT, KAREN L. · 2018 to 2020
$585k
NCI NIH HHS R21 CA229044NCI NIH HHS U01 CA168870NCI NIH HHS U01 CA226055
6 · The paper itself

Abstract

Tumor-specific glycosylation changes are an attractive target for the development of diagnostic and therapeutic applications. Periostin is a glycoprotein with high expression in many tumors of epithelial origin including ovarian cancer. Strategies to target the peptide portion of periostin as a diagnostic or therapeutic biomarker for cancer are limited due to increased expression of periostin in non-cancerous inflammatory conditions. Here, we have screened for antibody fragments that recognize the tumor-specific glycosylation present on glycoforms of periostin containing bisecting N-glycans in ovarian cancer using a yeast-display library of antibody fragments, while subtracting those that bind to the periostin protein with glycoforms found in non-malignant cell types. We generated a biotinylated form of a fully human scFv antibody (scFvC9) that targets the bisecting N-glycans expressed by cancer cells. Validation studies in vitro and in vivo using scFvC9 indicate this antibody can be useful for the development of diagnostic, imaging, and therapeutic applications for cancers that express the antigen.

Indexed as

AnimalsBlotting, WesternCell Adhesion MoleculesCell Line, TumorFemaleGlycosylationHumansImmunochemistryImmunoglobulin FragmentsMagnetic Resonance ImagingMiceOvarian NeoplasmsPeptide LibraryPolysaccharidesSingle-Chain AntibodiesCell Adhesion MoleculesImmunoglobulin FragmentsPeptide LibraryPolysaccharidesPOSTN protein, humanPostn protein, mouseSingle-Chain Antibodies

Identifiers

PMID30911061
PMCPMC6433917
OpenAlexW2924578535

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.