Evidence map›Paper›PMID 21795357›Full record

ArticleJournal of virology2011

Galectin-1 binds to influenza virus and ameliorates influenza virus pathogenesis.

Mei-Lin Yang, Yu-Hung Chen, Shainn-Wei Wang, Yen-Jang Huang, Chia-Hsing Leu, Nai-Chi Yeh, Chun-Yen Chu, Chia-Cheng Lin, Gia-Shing Shieh, Yuh-Ling Chen and 4 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

67 citing papers in PubMed, 127 citations in OpenAlex.

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7 more citing papers are in PubMed but not listed here.

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 at 4 institutions in 1 country.

Mei-Lin YangInstitute of Basic Medical Science, National Cheng Kung University Medical College, Tainan, Taiwan.
Yu-Hung Chen
Shainn-Wei Wang
Yen-Jang Huang
Chia-Hsing Leu
Nai-Chi Yeh
Chun-Yen Chu
Chia-Cheng Lin
Gia-Shing Shieh
Yuh-Ling Chen
Jen-Ren Wang
Ching-Ho Wang
Chao-Liang Wu
Ai-Li Shiau
National Cheng Kung University · TWNational Taiwan University · TWMinistry of Health and Welfare · TWNational Pingtung University of Science and Technology · TW

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI PAULSON, JAMES C · 2001 to 2010
$80.3M
NIGMS NIH HHS GM62116NIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

Innate immune response is important for viral clearance during influenza virus infection. Galectin-1, which belongs to S-type lectins, contains a conserved carbohydrate recognition domain that recognizes galactose-containing oligosaccharides. Since the envelope proteins of influenza virus are highly glycosylated, we studied the role of galectin-1 in influenza virus infection in vitro and in mice. We found that galectin-1 was upregulated in the lungs of mice during influenza virus infection. There was a positive correlation between galectin-1 levels and viral loads during the acute phase of viral infection. Cells treated with recombinant human galectin-1 generated lower viral yields after influenza virus infection. Galectin-1 could directly bind to the envelope glycoproteins of influenza A/WSN/33 virus and inhibit its hemagglutination activity and infectivity. It also bound to different subtypes of influenza A virus with micromolar dissociation constant (K(d)) values and protected cells against influenza virus-induced cell death. We used nanoparticle, surface plasmon resonance analysis and transmission electron microscopy to further demonstrate the direct binding of galectin-1 to influenza virus. More importantly, we show for the first time that intranasal treatment of galectin-1 could enhance survival of mice against lethal challenge with influenza virus by reducing viral load, inflammation, and apoptosis in the lung. Furthermore, galectin-1 knockout mice were more susceptible to influenza virus infection than wild-type mice. Collectively, our results indicate that galectin-1 has anti-influenza virus activity by binding to viral surface and inhibiting its infectivity. Thus, galectin-1 may be further explored as a novel therapeutic agent for influenza.

Indexed as

AnimalsAntiviral AgentsDisease Models, AnimalFemaleGalectin 1Influenza A virusKineticsLungMiceMice, Inbred C57BLMicroscopy, Electron, TransmissionOrthomyxoviridae InfectionsProtein BindingRodent DiseasesSurface Plasmon ResonanceSurvival AnalysisAntiviral AgentsGalectin 1

Identifiers

PMID21795357
PMCPMC3196456
OpenAlexW2155848597

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.