Evidence map›Paper›PMID 33024040›Full record

ArticlemBio2020

Structure-Based Modification of an Anti-neuraminidase Human Antibody Restores Protection Efficacy against the Drifted Influenza Virus.

Haihai Jiang, Weiyu Peng, Jianxun Qi, Yan Chai, Hao Song, Yuhai Bi, Pramila Rijal, Haiyuan Wang, Babayemi O Oladejo, Jinhua Liu and 4 more

Open access · goldAbstract read
In one paragraph

Article in mBio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 34 citations in OpenAlex.

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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 at 4 institutions in 2 countries.

Haihai Jiang *College of Veterinary Medicine, China Agricultural University, Beijing, China.
Weiyu Peng *College of Veterinary Medicine, China Agricultural University, Beijing, China.
Jianxun QiCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS), Beijing, China.ORCID 0000-0002-9358-4732
Yan ChaiCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS), Beijing, China.
Hao SongResearch Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing, China.ORCID 0000-0002-2811-0370
Yuhai BiCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS), Beijing, China.
Pramila RijalCenter for translational Immunology, Chinese Academy of Medical Science Oxford Institute, Nuffield Department of Medicine, Oxford University, Oxford, United Kingdom.
Haiyuan WangCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS), Beijing, China.
Babayemi O OladejoCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS), Beijing, China.
Jinhua LiuCollege of Veterinary Medicine, China Agricultural University, Beijing, China.ORCID 0000-0002-4128-1043
Yi ShiCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CAS), Beijing, China.
George F GaoCollege of Veterinary Medicine, China Agricultural University, Beijing, China gaof@im.ac.cn twosned@googlemail.com.
Alain R TownsendCenter for translational Immunology, Chinese Academy of Medical Science Oxford Institute, Nuffield Department of Medicine, Oxford University, Oxford, United Kingdom gaof@im.ac.cn twosned@googlemail.com.
Yan WuResearch Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing, China.
Chinese Academy of Sciences · CNUniversity of Oxford · GBCapital Medical University · CNChina Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here, we investigate a monoclonal antibody, Z2B3, isolated from an H7N9-infected patient, that exhibited cross-reactivity to both N9 (group 2) and a broad range of seasonal and avian N1 (group 1) proteins but lost activity to the N1 with the substitution K432E. This substitution exists in 99.25% of seasonal influenza strains after 2013. The NA-Z2B3 complex structures indicated that Z2B3 binds within the conserved active site of the neuraminidase (NA) protein. A salt bridge between D102 in Z2B3 and K432 in NA plays an important role in binding. Structure-based modification of Z2B3 with D102R in heavy chain reversed the salt bridge and restored the binding and inhibition of N1 with E432. Furthermore, Z2B3-D102R can protect mice from A/Serbia/NS-601/2014 H1N1 virus (NA contains E432) infection while the wild-type Z2B3 antibody shows no protection. This study demonstrates that a broadly reactive and protective antibody to NA can be in principle edited to restore binding and inhibition to recently drifted N1 NA and regain protection against the variant influenza strain.

Indexed as

AnimalsAntibodies, MonoclonalAntibodies, ViralAntigens, ViralBinding Sites, AntibodyCross ReactionsCrystallographyFemaleHumansInfluenza A Virus, H1N1 SubtypeInfluenza A Virus, H7N9 SubtypeInfluenza, HumanMice, Inbred BALB CNeuraminidaseOrthomyxoviridae InfectionsViral ProteinsAntibodies, MonoclonalAntibodies, ViralAntigens, ViralNA protein, influenza A virusNeuraminidaseViral Proteinsinfluenzaneuraminidaseneutralizing antibodystructure-based modification

Identifiers

PMID33024040
PMCPMC7542365
OpenAlexW3092120429

What OpenQuestion holds

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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.