Evidence map›Paper›PMID 34335603›Full record

ArticleFrontiers in immunology2021

Site-Specific Glycan-Masking/Unmasking Hemagglutinin Antigen Design to Elicit Broadly Neutralizing and Stem-Binding Antibodies Against Highly Pathogenic Avian Influenza H5N1 Virus Infections.

Ting-Hsuan Chen, Ya-Lin Yang, Jia-Tsrong Jan, Chung-Chu Chen, Suh-Chin Wu

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

10 citing papers in PubMed, 12 citations in OpenAlex.

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  10. Engineering recombinantly expressed lectin-based antiviral agents.Frontiers in cellular and infection microbiology · 2022
    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

5 authors at 3 institutions in 1 country.

Ting-Hsuan ChenInstitute of Biotechnology, National Tsing Hua University, Hsinchu, Taiwan.
Ya-Lin YangInstitute of Biotechnology, National Tsing Hua University, Hsinchu, Taiwan.
Jia-Tsrong JanGenomics Research Center, Academia Sinica, Taipei, Taiwan.
Chung-Chu ChenDepartment of Internal Medicine, MacKay Memorial Hospital, Hsinchu, Taiwan.
Suh-Chin WuInstitute of Biotechnology, National Tsing Hua University, Hsinchu, Taiwan.
National Tsing Hua University · TWGenomics Research Center, Academia Sinica · TWMinghsin University of Science and Technology · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The highly pathogenic avian influenza (HPAI) H5N1 viruses with the capability of transmission from birds to humans have a serious impact on public health. To date, HPAI H5N1 viruses have evolved into ten antigenically distinct clades that could cause a mismatch of vaccine strains and reduce vaccine efficacy. In this study, the glycan masking and unmasking strategies on hemagglutinin antigen were used for designing two antigens: H5-dm/st2 and H5-tm/st2, and investigated for their elicited immunity using two-dose recombinant H5 (rH5) immunization and a first-dose adenovirus vector prime, followed by a second-dose rH5 protein booster immunization. The H5-dm/st2 antigen was found to elicit broadly neutralizing antibodies against different H5N1 clade/subclade viruses, as well as more stem-binding antibodies to inhibit HA-facilitated membrane fusion activity. Mice immunized with the H5-dm/st2 antigen had a higher survival rate when challenged with homologous and heterologous clades of H5N1 viruses. Mutant influenza virus replaced with the H5-dm/st2 gene generated by reverse genetics (RG) technology amplified well in MDCK cells and embryonated chicken eggs. Again, the inactivated H5N1-dm/st2 RG virus elicited more potent cross-clade neutralizing and anti-fusion antibodies in sera. Therefore, the H5N1-dm/st2 RG virus with the site-specific glycan-masking on the globular head and the glycan-unmasking on the stem region of H5 antigen can be used for further development of cross-protective H5N1 vaccines.

Indexed as

Immunodominant EpitopesImmunogenicity, VaccineAnimalsAntibodies, ViralAntigens, ViralBroadly Neutralizing AntibodiesChick EmbryoDisease Models, AnimalDogsFemaleHemagglutinin Glycoproteins, Influenza VirusImmunizationInfluenza A Virus, H5N1 SubtypeInfluenza VaccinesMadin Darby Canine Kidney CellsMiceAntibodies, ViralAntigens, ViralBroadly Neutralizing AntibodiesHemagglutinin Glycoproteins, Influenza VirusImmunodominant EpitopesInfluenza VaccinesPolysaccharidesglycan maskingglycan unmaskingH5N1hemagglutininvaccine

Identifiers

PMID34335603
PMCPMC8317614
OpenAlexW3178456649

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.