Evidence map›Paper›PMID 29035787›Full record

ArticleVirology2018

Identification of N-linked glycosylation sites in the spike protein and their functional impact on the replication and infectivity of coronavirus infectious bronchitis virus in cell culture.

Jie Zheng, Yoshiyuki Yamada, To Sing Fung, Mei Huang, Raymond Chia, Ding Xiang Liu

Abstract read
In one paragraph

Article in Virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

38 citing papers in PubMed, 84 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

6 authors at 3 institutions in 2 countries.

Jie ZhengSouth China Agricultural University, Guangdong Province Key Laboratory Microbial Signals & Disease Co, and Integrative Microbiology Research Centre, Guangzhou 510642, Guangdong, People's Republic of China; School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 63755.
Yoshiyuki YamadaInstitute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673.
To Sing FungSouth China Agricultural University, Guangdong Province Key Laboratory Microbial Signals & Disease Co, and Integrative Microbiology Research Centre, Guangzhou 510642, Guangdong, People's Republic of China.
Mei HuangSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 63755.
Raymond ChiaInstitute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673.
Ding Xiang LiuSouth China Agricultural University, Guangdong Province Key Laboratory Microbial Signals & Disease Co, and Integrative Microbiology Research Centre, Guangzhou 510642, Guangdong, People's Republic of China. Electronic address: dxliu0001@163.com.
South China Agricultural University · CNInstitute of Molecular and Cell Biology · SGNanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Spike (S) glycoprotein on the viral envelope is the main determinant of infectivity. The S protein of coronavirus infectious bronchitis virus (IBV) contains 29 putative asparagine(N)-linked glycosylation sites. These post-translational modifications may assist in protein folding and play important roles in the functionality of S protein. In this study, we used bioinformatics tools to predict N-linked glycosylation sites and to analyze their distribution in IBV strains and variants. Among these sites, 8 sites were confirmed in the S protein extracted from partially purified virus particles by proteomics approaches. N-D and N-Q substitutions at 13 predicted sites were introduced into an infectious clone system. The impact on S protein-mediated cell-cell fusion, viral recovery and infectivity was assessed, leading to the identification of sites essential for the functions of IBV S protein. Further characterization of these and other uncharacterized sites may reveal novel aspects of N-linked glycosylation in coronavirus replication and pathogenesis.

Indexed as

Virus InternalizationVirus ReplicationAmino Acid SubstitutionAnimalsChlorocebus aethiopsComputational BiologyDNA Mutational AnalysisGlycosylationInfectious bronchitis virusProteomicsSpike Glycoprotein, CoronavirusVero CellsVirus CultivationSpike Glycoprotein, Coronavirusspike protein, avian infectious bronchitis virusCell-cell fusionCloneCoronavirusInfectious bronchitis virusInfectious cDNAN-linked glycosylationSpike proteinVirus infectivity

Identifiers

PMID29035787
PMCPMC7112133
OpenAlexW2761706043

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.