Evidence map›Paper›PMID 32552895›Full record

ArticleBMC biotechnology2020

Evaluation of Hydra HALT-1 as a toxin moiety for recombinant immunotoxin.

William F Jiemy, Lih Fhung Hiew, Hong Xi Sha, Lionel L A In, Jung Shan Hwang

Open access · goldAbstract read
In one paragraph

Article in BMC biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Advancements in antibody-drug conjugates as cancer therapeutics.Journal of the National Cancer Center · 2025
    Review
  2. Article
  3. Article
  4. Preparation of a novel EGFR specific immunotoxin and its efficacy of anti-colorectal cancer in vitro and in vivo.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2021
    Article
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

5 authors at 2 institutions in 1 country.

William F JiemyDepartment of Biotechnology, Faculty of Applied Sciences, UCSI University, 56000, Kuala Lumpur, Malaysia.
Lih Fhung HiewDepartment of Biological Sciences, School of Science and Technology, Sunway University, No. 5, Jalan Universiti, Bandar Sunway, 47500 Selangor Darul Ehsan, Malaysia.
Hong Xi ShaDepartment of Biological Sciences, School of Science and Technology, Sunway University, No. 5, Jalan Universiti, Bandar Sunway, 47500 Selangor Darul Ehsan, Malaysia.
Lionel L A InDepartment of Biotechnology, Faculty of Applied Sciences, UCSI University, 56000, Kuala Lumpur, Malaysia.
Jung Shan HwangDepartment of Medical Sciences, School of Healthcare and Medical Sciences, Sunway University, No. 5, Jalan Universiti, Bandar Sunway, 47500 Selangor Darul Ehsan, Malaysia. hwangjs@sunway.edu.my.ORCID 0000-0002-0908-2036
Sunway University · MYUCSI University · MY

Funding

UCSI University Proj-In-FAS-020
6 · The paper itself

Abstract

backgroundImmunotoxin is a hybrid protein consisting of a toxin moiety that is linked to a targeting moiety for the purpose of specific elimination of target cells. Toxins used in traditional immunotoxins are practically difficult to be produced in large amount, have poor tissue penetration and a complex internalization process. We hypothesized that the smaller HALT-1, a cytolysin derived from Hydra magnipapillata, can be used as the toxin moiety in construction of a recombinant immunotoxin.

resultsIn this study, pro-inflammatory macrophage was selected as the target cell due to its major roles in numerous inflammatory and autoimmune disorders. We aimed to construct macrophage-targeted recombinant immunotoxins by combining HALT-1 with anti-CD64-scFv in two orientations, and to assess whether their cytotoxic activity and binding capability could be preserved upon molecular fusion. The recombinant immunotoxins, HALT-1-scFv and scFv-HALT-1, were successfully constructed and expressed in Escherichia coli (E. coli). Our data showed that HALT-1 still exhibited significant cytotoxicity against CD64

conclusionsHALT-1 could be fused with anti-CD64-scFv via a fsexible polypeptide linker. Upon the successful production of this recombinant HALT-1 scFv fusion protein, HALT-1 was proven effective for killing two human cell lines. Hence, this preliminary study strongly suggested that HALT-1 holds potential as the toxin moiety in therapeutic cell targeting.

Indexed as

AnimalsCell LineCnidariaEscherichia coliHumansHydraImmunotoxinsReceptors, IgGSingle-Chain AntibodiesToxins, BiologicalImmunotoxinsReceptors, IgGSingle-Chain AntibodiesToxins, BiologicalActinoporinCnidariaImmunotoxinProinflammatorySingle chain fragment variableα-Pore forming toxin

Identifiers

PMID32552895
PMCPMC7301450
OpenAlexW3036369753

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.