Evidence map›Paper›PMID 33606171›Full record

ArticleVirus genes2021

The effect of single amino acid substitution at position 220 in the hemagglutinin glycoprotein on avian influenza H7N9 candidate vaccine virus.

Liqi Liu, Zi Li, Jianfang Zhou, Jian Lu, Xiyan Li, Jia Liu, Ning Xiao, Dayan Wang

Abstract read
PubMed Publisher
In one paragraph

Article in Virus genes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

3 citing papers in PubMed, 4 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

8 authors at 1 institution in 1 country.

Liqi LiuChinese National Influenza Center, National Institute for Viral Disease Control and Prevention, China CDC, Beijing, People's Republic of China.
Zi LiChinese National Influenza Center, National Institute for Viral Disease Control and Prevention, China CDC, Beijing, People's Republic of China.
Jianfang ZhouChinese National Influenza Center, National Institute for Viral Disease Control and Prevention, China CDC, Beijing, People's Republic of China.
Jian LuChinese National Influenza Center, National Institute for Viral Disease Control and Prevention, China CDC, Beijing, People's Republic of China.
Xiyan LiChinese National Influenza Center, National Institute for Viral Disease Control and Prevention, China CDC, Beijing, People's Republic of China.
Jia LiuChinese National Influenza Center, National Institute for Viral Disease Control and Prevention, China CDC, Beijing, People's Republic of China.
Ning XiaoChinese National Influenza Center, National Institute for Viral Disease Control and Prevention, China CDC, Beijing, People's Republic of China.
Dayan WangChinese National Influenza Center, National Institute for Viral Disease Control and Prevention, China CDC, Beijing, People's Republic of China. dayanwang@cnic.org.cn.ORCID http://orcid.org/0000-0002-4990-1016
Chinese Center For Disease Control and Prevention · CN

Funding

Gansu Provincial Health Industry Scientific Research Project GSWSKY2017-28National Key Research and Development Program 2020ZX10101016National Mega-projects for Infectious Diseases 2017ZX10303401-004National Mega-projects for Infectious Diseases 2018ZX10305409-004-002
6 · The paper itself

Abstract

Influenza vaccines represent the most effective preventive strategy to control influenza virus infections; however, adaptive mutations frequently occur in the hemagglutinin (HA) glycoprotein during the preparation of candidate vaccine virus and production of vaccine in embryonated eggs. In our previous study, we constructed candidate vaccine virus (HA-R) to match the highly pathogenic avian influenza H7N9 viruses A/Guangdong/17SF003/2016 as part of a pandemic preparedness program. However, mixed amino acids (R, G, and I) were presented at position 220 (H3 numbering) in HA during passage in embryonated eggs. The residue at position 220 is located close to the receptor-binding site and the biological characteristics of this site remain to be elucidated. Therefore, in this study, using reverse genetics, we constructed two viruses carrying the single substitution in position 220 of HA (HA-G and HA-I) and evaluated the biological effects of substitution (R with G/I) on receptor binding, neuraminidase (NA) activity, growth characteristics, genetic stability, and antigenicity. The results revealed both mutant viruses exhibited lower HA binding affinities to two receptor types (sialic acid in alpha2,3- and alpha2,6-linkage to galactose, P < 0.001) and significant better growth characteristics compared to HA-R in two cells. Moreover, under similar NA enzymatic activity, the two mutant viruses eluted more easily from agglutinated erythrocytes than HA-R. Collectively, these results implied the balance of HA and NA in mutant viruses was a stronger determinant of viral growth than the individual amino acid in the HA position 220 in HA-R without strong binding between HA and sialylated receptors. Importantly, both the substitutions conferred altered antigenicity to the mutant viruses. In conclusion, amino acid substitutions at position 220 can substantially influence viral biological properties.

Indexed as

Amino Acid SubstitutionAnimalsDogsHemagglutinin Glycoproteins, Influenza VirusInfluenza A Virus, H7N9 SubtypeInfluenza VaccinesMadin Darby Canine Kidney CellsMutagenesisN-Acetylneuraminic AcidNeuraminidaseReassortant VirusesReverse GeneticsHemagglutinin Glycoproteins, Influenza VirusInfluenza VaccinesN-Acetylneuraminic AcidNeuraminidaseAntigenicityAvian influenza H7N9 virusGrowth characteristicHemagglutininReceptor affinitySubstitution

Identifiers

PMID33606171
OpenAlexW3131982544

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Registered trials

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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.