Evidence map›Paper›PMID 24858932›Full record

ArticlePloS one2014

Glycoengineering of interferon-β 1a improves its biophysical and pharmacokinetic properties.

Kyoung Song, In-Soo Yoon, Nam Ah Kim, Dong-Hwan Kim, Jongmin Lee, Hee Jung Lee, Saehyung Lee, Sunghyun Choi, Min-Koo Choi, Ha Hyung Kim and 4 more

Abstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

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  15. Review
  16. Article
  17. Improving Immunotherapy Through Glycodesign.Frontiers in immunology · 2018
    Review
  18. Article
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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

14 authors.

Kyoung SongCollege of Pharmacy and Research Institute of Pharmaceutical Sciences, Seoul National University, Seoul, Republic of Korea; Research Institute of Reference Biolabs. Inc., Seoul, Republic of Korea.
In-Soo YoonCollege of Pharmacy and Natural Medicine Research Institute, Mokpo National University, Jeonnam, Republic of Korea.
Nam Ah KimCollege of Pharmacy, Dongguk University-Seoul, Gyeonggi-do, Republic of Korea.
Dong-Hwan KimCollege of Pharmacy and Research Institute of Pharmaceutical Sciences, Seoul National University, Seoul, Republic of Korea.
Jongmin LeePanGen Biotech Inc., Gyeonggi-do, Republic of Korea.
Hee Jung LeeResearch Institute of Reference Biolabs. Inc., Seoul, Republic of Korea.
Saehyung LeeCollege of Pharmacy and Research Institute of Pharmaceutical Sciences, Seoul National University, Seoul, Republic of Korea.
Sunghyun ChoiResearch Institute of Reference Biolabs. Inc., Seoul, Republic of Korea.
Min-Koo ChoiCollege of Pharmacy, DanKook University, Chungnam, Republic of Korea.
Ha Hyung KimBiotherapeutics and Glycomics Laboratory, College of Pharmacy, Chung-Ang University, Seoul, Republic of Korea.
Seong Hoon JeongCollege of Pharmacy, Dongguk University-Seoul, Gyeonggi-do, Republic of Korea.
Woo Sung SonCollege of Pharmacy, CHA University, Gyeonggi-do, Republic of Korea.
Dae-Duk KimCollege of Pharmacy and Research Institute of Pharmaceutical Sciences, Seoul National University, Seoul, Republic of Korea.
Young Kee ShinCollege of Pharmacy and Research Institute of Pharmaceutical Sciences, Seoul National University, Seoul, Republic of Korea; Institutes of Entrepreneurial BioConvergence, Seoul National University, Seoul, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The purpose of this study was to develop a biobetter version of recombinant human interferon-β 1a (rhIFN-β 1a) to improve its biophysical properties, such as aggregation, production and stability, and pharmacokinetic properties without jeopardizing its activity. To achieve this, we introduced additional glycosylation into rhIFN-β 1a via site-directed mutagenesis. Glycoengineering of rhIFN-β 1a resulted in a new molecular entity, termed R27T, which was defined as a rhIFN-β mutein with two N-glycosylation sites at 80th (original site) and at an additional 25th amino acid due to a mutation of Thr for Arg at position 27th of rhIFN-β 1a. Glycoengineering had no effect on rhIFN-β ligand-receptor binding, as no loss of specific activity was observed. R27T showed improved stability and had a reduced propensity for aggregation and an increased half-life. Therefore, hyperglycosylated rhIFN-β could be a biobetter version of rhIFN-β 1a with a potential for use as a drug against multiple sclerosis.

Indexed as

Biophysical PhenomenaMutagenesis, Site-DirectedAnimalsBinding SitesGlycosylationHumansInterferon-betaInterferon beta-1aLigandsMonosaccharidesN-Acetylneuraminic AcidProtein ConformationProtein StabilityRatsSolubilitySubstrate SpecificityInterferon-betaInterferon beta-1aLigandsMonosaccharidesN-Acetylneuraminic Acid

Identifiers

PMID24858932
PMCPMC4032242

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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.