Evidence map›Paper›PMID 28507200›Full record

ArticleBioscience reports2017

Effects of microvirin monomers and oligomers on hepatitis C virus.

Yuan-Qin Min, Xu-Chu Duan, Yi-Dan Zhou, Anna Kulinich, Wang Meng, Zhi-Peng Cai, Hong-Yu Ma, Li Liu, Xiao-Lian Zhang, Josef Voglmeir

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioscience reports, 2017. 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
–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

5 citing papers in PubMed.

  1. Lectins and lectibodies: potential promising antiviral agents.Cellular & molecular biology letters · 2022
    Review
  2. Review
  3. Article
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  5. 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

10 authors.

Yuan-Qin MinState Key Laboratory of Virology, Department of Immunology, Hubei Province Key Laboratory of Allergy and Immunology, School of Medicine, Wuhan University, Wuhan, People's Republic of China.
Xu-Chu DuanGlycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, People's Republic of China.
Yi-Dan ZhouDepartment of Microbiology, School of Molecular and Cellular Biology, University of Illinois at Urbana-Champaign, IL 61801, U.S.A.
Anna KulinichGlycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, People's Republic of China.
Wang MengGlycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, People's Republic of China.
Zhi-Peng CaiGlycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, People's Republic of China.
Hong-Yu MaDepartment of Plant Pathology, Nanjing Agricultural University, Nanjing, People's Republic of China.
Li LiuGlycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, People's Republic of China.
Xiao-Lian ZhangState Key Laboratory of Virology, Department of Immunology, Hubei Province Key Laboratory of Allergy and Immunology, School of Medicine, Wuhan University, Wuhan, People's Republic of China zhangxiaolian@whu.edu.cn josef.voglmeir@njau.edu.cn.
Josef VoglmeirGlycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, People's Republic of China zhangxiaolian@whu.edu.cn josef.voglmeir@njau.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microvirin (MVN) is a carbohydrate-binding protein which shows high specificity for high-mannose type N-glycan structures. In the present study, we tried to identify whether MVN could bind to high-mannose containing hepatitis C virus (HCV) envelope glycoproteins, which are heavily decorated high-mannose glycans. In addition, recombinantly expressed MVN oligomers in di-, tri- and tetrameric form were evaluated for their viral inhibition. MVN oligomers bound more efficiently to HCV virions, and displayed in comparison with the MVN monomer a higher neutralization potency against HCV infection. The antiviral effect was furthermore affected by the peptide linker sequence connecting the MVN monomers. The results indicate that MVN oligomers such as trimers and tetramers may be used as future neutralization agents against HCV infections.

Indexed as

Antiviral AgentsBacterial ProteinsCell LineCloning, MolecularHepacivirusHepatitis CHumansMannose-Binding LectinMicrocystisProtein MultimerizationRecombinant ProteinsAntiviral AgentsBacterial ProteinsMannose-Binding Lectinmicrovirin protein, Microcystis aeruginosaRecombinant Proteinshepatitis C virushigh-mannose glycanlectin oligomerMicrovirin

Identifiers

PMID28507200
PMCPMC6434159

What OpenQuestion holds

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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.