Evidence map›Paper›PMID 31479875›Full record

ArticleCytokine2020

Structure-based glycoengineering of interferon lambda 4 enhances its productivity and anti-viral potency.

Jae-Hee Chung, Seon-Hui Hong, Nari Seo, Tae-Shin Kim, Hyun Joo An, Pedro Lee, Eui-Cheol Shin, Ho Min Kim

Abstract read
In one paragraph

Article in Cytokine, 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
–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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. 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

8 authors.

Jae-Hee ChungDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea.
Seon-Hui HongBiomedical Science and Engineering Interdisciplinary Program, Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea.
Nari SeoGraduate School of Analytical Science & Technology, Chungnam National University, Daejeon 34134, Republic of Korea.
Tae-Shin KimGraduate School of Medical Science & Engineering, Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea.
Hyun Joo AnGraduate School of Analytical Science & Technology, Chungnam National University, Daejeon 34134, Republic of Korea.
Pedro LeeGraduate School of Medical Science & Engineering, Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea.
Eui-Cheol ShinBiomedical Science and Engineering Interdisciplinary Program, Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea; Graduate School of Medical Science & Engineering, Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea. Electronic address: ecshin@kaist.ac.kr.
Ho Min KimBiomedical Science and Engineering Interdisciplinary Program, Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea; Graduate School of Medical Science & Engineering, Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea; Center for Biomolecular & Cellular Structure, Institute for Basic Science (IBS), Daejeon 34126, Republic of Korea. Electronic address: hm_kim@kaist.ac.kr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interferon lambda 4 (IFNλ4) has been recently known and studied for its role in hepatitis C virus (HCV) infection, but its clinical potential is significantly hampered due to its poor expression in vitro. Our study reports the successful production of IFNλ4 from a mammalian cell line through a glycoengineering and structure-based approach. We introduced de novo N-glycosylation of IFNλ4, guided by structural analysis, and produced IFNλ4 variants in Expi293F that displayed improved expression and potency. To preserve the structure and functionality of IFNλ4, the model structure of the IFNλ4 signaling complex was analyzed and the N-glycosylation candidate sites were selected. The receptor binding activity of engineered IFNλ4 variants and their receptor-mediated signaling pathway were similar to the E. coli version of IFNλ4 (eIFNλ4), while the antiviral activity and induction levels of interferon-stimulated gene (ISG) were all more robust in our variants. Our engineered IFNλ4 variants may be further developed for clinical applications and utilized in basic research to decipher the immunological roles of IFNλ4.

Indexed as

Amino Acid SequenceEscherichia coliGene ExpressionGene Expression RegulationGlycosylationHEK293 CellsHepacivirusHepatitis CHumansInterferon LambdaInterferonsInterleukinsKineticsMetabolic EngineeringProtein BindingRecombinant ProteinsIFNL4 protein, humanInterferon LambdaInterferonsInterleukinsRecombinant ProteinsAnti-viral activityGlycoengineeringHomology modelingIFNλ4Type III interferon signaling

Identifiers

PMID31479875
PMCPMC7129780

What OpenQuestion holds

Textmetadata
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.