Evidence map›Paper›PMID 30339712›Full record

ArticlePLoS pathogens2018

Nucleolin mediates the internalization of rabbit hemorrhagic disease virus through clathrin-dependent endocytosis.

Jie Zhu, Qiuhong Miao, Jingyu Tang, Xiaoxue Wang, Dandan Dong, Teng Liu, Ruibin Qi, Zhibiao Yang, Guangqing Liu

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Characterisation ofInternational journal of molecular sciences · 2024
    Review
  5. Article
  6. Article
  7. Nucleolin binds to and regulates transcription of hepatitis B virus covalently closed circular DNA minichromosome.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Article
  10. Nucleolin: a cell portal for viruses, bacteria, and toxins.Cellular and molecular life sciences : CMLS · 2022
    Review
  11. Seneca Valley Virus 3CMicrobiology spectrum · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Viruses · 2019
    Review
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

9 authors at 2 institutions in 2 countries.

Jie ZhuShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, P. R. China.
Qiuhong MiaoShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, P. R. China.
Jingyu TangShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, P. R. China.
Xiaoxue WangShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, P. R. China.
Dandan DongShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, P. R. China.
Teng LiuShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, P. R. China.
Ruibin QiShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, P. R. China.
Zhibiao YangShanghai Key Laboratory of Veterinary Biotechnology, Shanghai Jiao Tong University, Shanghai, P. R. China.
Guangqing LiuShanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, P. R. China.ORCID 0000-0002-7116-3689
Shanghai Veterinary Research Institute · CNShanghai Jiao Tong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rabbit hemorrhagic disease virus (RHDV) is an important member of the Caliciviridae family and a highly lethal pathogen in rabbits. Although the cell receptor of RHDV has been identified, the mechanism underlying RHDV internalization remains unknown. In this study, the entry and post-internalization of RHDV into host cells were investigated using several biochemical inhibitors and RNA interference. Our data demonstrate that rabbit nucleolin (NCL) plays a key role in RHDV internalization. Further study revealed that NCL specifically interacts with the RHDV capsid protein (VP60) through its N-terminal residues (aa 285-318), and the exact position of the VP60 protein for the interaction with NCL is located in a highly conserved region (472Asp-Val-Asn474; DVN motif). Following competitive blocking of the interaction between NCL and VP60 with an artificial DVN peptide (RRTGDVNAAAGSTNGTQ), the internalization efficiency of the virus was markedly reduced. Moreover, NCL also interacts with the C-terminal residues of clathrin light chain A, which is an important component in clathrin-dependent endocytosis. In addition, the results of animal experiments also demonstrated that artificial DVN peptides protected most rabbits from RHDV infection. These findings demonstrate that NCL is involved in RHDV internalization through clathrin-dependent endocytosis.

Indexed as

EndocytosisVirus AssemblyAnimalsCaliciviridae InfectionsClathrinHemorrhagic Disease Virus, RabbitMaleMiceNucleolinPhosphoproteinsProtein ConformationRabbitsRNA-Binding ProteinsViral Structural ProteinsVirus InternalizationClathrinNucleolinPhosphoproteinsRNA-Binding Proteinsviral protein 60, rabbit hemorrhagic disease virusViral Structural Proteins

Identifiers

PMID30339712
PMCPMC6209375
OpenAlexW2895952839

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.