Evidence map›Paper›PMID 37004901›Full record

ArticleVirus research2023

Characterization of novel cell-penetrating peptides derived from the capsid protein of beak and feather disease virus.

Mikael Cristofer Sitinjak, Jui-Kai Chen, Chi-Young Wang

Open access · goldAbstract read
In one paragraph

Article in Virus research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. 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

3 authors at 1 institution in 1 country.

Mikael Cristofer SitinjakDepartment of Veterinary Medicine, College of Veterinary Medicine, National Chung Hsing University, 250 Kuo Kuang Road, Taichung 40227, Taiwan.
Jui-Kai ChenDepartment of Veterinary Medicine, College of Veterinary Medicine, National Chung Hsing University, 250 Kuo Kuang Road, Taichung 40227, Taiwan.
Chi-Young WangDepartment of Veterinary Medicine, College of Veterinary Medicine, National Chung Hsing University, 250 Kuo Kuang Road, Taichung 40227, Taiwan; The iEGG and Animal Biotechnology Center, National Chung Hsing University, 250 Kuo Kuang Road, Taichung 40227, Taiwan. Electronic address: cyoungwang@dragon.nchu.edu.tw.
National Chung Hsing University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Beak and feather disease virus (BFDV) is a 17-20 nm icosahedral virus belonging to the Circoviridae family. Psittacine beak and feather disease (PBFD) is caused by BFDV and its common symptoms include abnormal feather, beak, and claw development, as well as immunosuppression in various bird species. In this study, novel cell-penetrating peptides (CPPs) in the capsid protein (Cap) of BFDV were identified through bioinformatic analyses, after which they were experimentally characterized. The cell-penetrating activities of both CPP1 and CPP2 of BFDV were analyzed through flow cytometry and image analysis. The internalization of CPP1 and CPP2 was both dose- and time-dependent but their uptake efficiencies varied depending on the cell type. The cell-penetrating activities of BFDV CPP1 and CPP2 were both superior to that of a typical CPP-TAT originating from the viral protein of human immunodeficiency virus. The cellular uptake of 5 μM CPP1 was close to that of 25 μM TAT, albeit with less cytotoxicity. Using the identified CPPs, the pc-mCheery, pc-Rep, and pc-Cap plasmids were successfully delivered into the target cells for expression. Moreover, both the replication-associated protein with the tag and the Cap protein with the tag could also be successfully delivered into the cells by CPP1 and CPP2. Multiple endocytosis pathways and direct translocation were involved in the cell internalization of CPP1 and CPP2. Furthermore, the delivery of the apoptin gene using CPP1 and CPP2 effectively triggered apoptosis, thus confirming the potential of these CPPs as delivery vehicles. Similarly, green fluorescent protein (GFP) fused with CPP1 or CPP2 at their N-terminus successfully entered the cells. However, the cell internalization efficiency of CPP2-GFP was higher than that of CPP1-GFP. Taken together, our findings demonstrated that both CPP1 and CPP2 of BFDV have promising potential as novel CPPs.

Indexed as

Bird DiseasesCell-Penetrating PeptidesCircoviridae InfectionsCircovirusAnimalsBirdsCapsid ProteinsHumansCapsid ProteinsCell-Penetrating PeptidesCell-penetrating peptideFlow cytometryInternalization

Identifiers

PMID37004901
PMCPMC10194187
OpenAlexW4362507010

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.