Evidence map›Paper›PMID 33128033›Full record

ArticleCommunications biology2020

Aglycosylated antibody-producing mice for aglycosylated antibody-lectin coupled immunoassay for the quantification of tumor markers (ALIQUAT).

Nan-Ee Lee, Sun Hee Kim, Dae-Yeul Yu, Eui-Jeon Woo, Myung-Il Kim, Gi-Sang Seong, Sun Min Lee, Jeong-Heon Ko, Yong-Sam Kim

Abstract read
In one paragraph

Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

9 authors.

Nan-Ee LeeGenome Editing Research Center, KRIBB, Daejeon, 34141, Republic of Korea.
Sun Hee KimGenome Editing Research Center, KRIBB, Daejeon, 34141, Republic of Korea.
Dae-Yeul YuGenome Editing Research Center, KRIBB, Daejeon, 34141, Republic of Korea.
Eui-Jeon WooDepartment of Bio-molecular Science, KRIBB School of Bioscience, Korea University of Science and Technology (UST), Daejeon, 34113, Republic of Korea.ORCID 0000-0001-6983-0270
Myung-Il KimBioneer, Daejeon, 34302, Republic of Korea.
Gi-Sang SeongBioneer, Daejeon, 34302, Republic of Korea.
Sun Min LeeDepartment of Laboratory Medicine, Pusan National University Yangsan Hospital and School of Medicine, Gyeongnam, 50612, Republic of Korea.
Jeong-Heon KoGenome Editing Research Center, KRIBB, Daejeon, 34141, Republic of Korea. jhko@kribb.re.kr.
Yong-Sam KimGenome Editing Research Center, KRIBB, Daejeon, 34141, Republic of Korea. omsys1@kribb.re.kr.ORCID 0000-0002-3133-3954

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Targeting aberrant glycoforms has been validated for in vitro cancer diagnostic development, and several assays are currently in routine clinical use. Because N-glycans in Fc region of antibodies show cross-reactivity with various lectins, high-quality aglycosylated antibodies are exceptionally important for immunoassay platform-based quantitative measurements. Previously, aglycosylated antibody acquisition relied on incomplete, uneconomical and onerous enzymatic and chemical methods. Here, we edited four murine immunoglobulin G genes using adenine base-editing and homology-directed recombination (HDR)-mediated gene editing methods to generate aglycosylated antibody-producing mice. Resulting aglycosylated antibodies showed required analytical performances without compromised protein stability. Thus, this aglycosylated monoclonal antibody-lectin coupled immunoassay for the quantification of tumour markers (ALIQUAT) method can provide a robust, versatile and accessible immunoassay platform to quantify specific glycoforms in precision cancer diagnostics. Moreover, the engineered mice can be used as a host to produce various aglycosylated antibodies in a convenient and robust fashion, thereby expanding in vitro diagnostic development opportunities that utilize glycoforms as a disease-specific biomarkers.

Indexed as

alpha-FetoproteinsAnimalsAntibodies, MonoclonalBiomarkers, TumorEnzyme-Linked Immunosorbent AssayFucosyltransferasesGlycosylationHEK293 CellsHumansImmunoassayImmunoglobulin GLectinsMice, Inbred BALB CMice, Inbred C57BLMice, TransgenicProtein StabilityAFP protein, humanalpha-FetoproteinsAntibodies, MonoclonalBiomarkers, TumorFucosyltransferasesGlycoprotein 6-alpha-L-fucosyltransferaseImmunoglobulin GLectins

Identifiers

PMID33128033
PMCPMC7599229

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.