Evidence map›Paper›PMID 31180180›Full record

ArticleBiotechnology progress2019

Lectin bio-layer interferometry for assessing product quality of Fc- glycosylated immunoglobulin G.

Jakob Wallner, Bernhard Sissolak, Wolfgang Sommeregger, Nico Lingg, Gerald Striedner, Karola Vorauer-Uhl

Open access · hybridAbstract read
In one paragraph

Article in Biotechnology progress, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Label-free methods for opticalPhysical chemistry chemical physics : PCCP · 2021
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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 2 institutions in 1 country.

Jakob WallnerDepartment of Biotechnology, University of Natural Resources and Life Sciences, Vienna, Austria.
Bernhard SissolakResearch and Development, Bilfinger Industrietechnik Salzburg GmbH, Salzburg, Austria.ORCID 0000-0002-5267-5005
Wolfgang SommereggerResearch and Development, Bilfinger Industrietechnik Salzburg GmbH, Salzburg, Austria.
Nico LinggDepartment of Biotechnology, University of Natural Resources and Life Sciences, Vienna, Austria.
Gerald StriednerDepartment of Biotechnology, University of Natural Resources and Life Sciences, Vienna, Austria.
Karola Vorauer-UhlDepartment of Biotechnology, University of Natural Resources and Life Sciences, Vienna, Austria.
BOKU University · ATFachhochschule Salzburg · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation, as the most prominent posttranslational modification, is recognized as an important quality attribute of monoclonal antibodies affected by various bioprocess parameters and cellular physiology. A method of lectin-based bio-layer interferometry (LBLI) to relatively rank galactosylation and fucosylation levels was developed. For this purpose, Fc-glycosylated immunoglobulin G (IgG) was recombinantly produced with varying bioprocess conditions in 15 L bioreactor and accumulated IgG was harvested. The reliability, the robustness and the applicability of LBLI to different samples has been proven. Data obtained from LC-MS analysis served as reference and were compared to the LBLI results. The introduced method is based on non-fluidic bio-layer interferometry (BLI), which becomes recently a standard tool for determining biomolecular interactions in a label-free, real-time and high-throughput manner. For the intended purpose, biotinylated lectins were immobilized on disposable optical fiber streptavidin (SA) biosensor tips. Aleuria aurantia lectin (AAL) was used to detect the core fucose and Ricinus communis agglutinin 120 (RCA120) to determine galactosylation levels. In our case study it could be shown that fucosylation was not affected by variations in glucose feed concentration and cultivation temperature. However, the galactosylation could be correlated with the ratio of mean specific productivity (q

Indexed as

LightAnimalsCHO CellsCricetulusGlycoproteinsImmunoglobulin Fc FragmentsImmunoglobulin GInterferometryLectinsGlycoproteinsglycosylated IgGImmunoglobulin Fc FragmentsImmunoglobulin GLectinsbio-layer interferometryCHO cell culturefucosylationgalactosylationglycosylation

Identifiers

PMID31180180
PMCPMC6852021
OpenAlexW2949240876

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.