Evidence map›Paper›PMID 26805881›Full record

ArticleToxins2016

Recombinant HSA-CMG2 Is a Promising Anthrax Toxin Inhibitor.

Liangliang Li, Qiang Guo, Ju Liu, Jun Zhang, Ying Yin, Dayong Dong, Ling Fu, Junjie Xu, Wei Chen

Open access · goldAbstract read
In one paragraph

Article in Toxins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.5field-weighted citation impact, top 29% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. 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

9 authors at 1 institution in 1 country.

Liangliang LiLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, Beijing 100071, China. byebyelll@163.com.
Qiang GuoLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, Beijing 100071, China. jackyguo@163.com.
Ju LiuLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, Beijing 100071, China. 18701522421@163.com.
Jun ZhangLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, Beijing 100071, China. justforhere@126.com.
Ying YinLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, Beijing 100071, China. yinying1028@sina.cn.
Dayong DongLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, Beijing 100071, China. akta100@sina.com.
Ling FuLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, Beijing 100071, China. fuling3436@163.com.
Junjie XuLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, Beijing 100071, China. xujunjie@sina.com.
Wei ChenLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, Beijing 100071, China. cw0226@foxmail.com.
National Vaccine and Serum Institute · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Anthrax toxin is the major virulence factor produced by Bacillus anthracis. Protective antigen (PA) is the key component of the toxin and has been confirmed as the main target for the development of toxin inhibitors. The inhibition of the binding of PA to its receptor, capillary morphogenesis protein-2 (CMG2), can effectively block anthrax intoxication. The recombinant, soluble von Willebrand factor type A (vWA) domain of CMG2 (sCMG2) has demonstrated potency against anthrax toxin. However, the short half-life of sCMG2 in vivo is a disadvantage for its development as a new anthrax drug. In the present study, we report that HSA-CMG2, a protein combining human serum albumin (HSA) and sCMG2, produced in the Pichia pastoris expression system prolonged the half-life of sCMG2 while maintaining PA binding ability. The IC50 of HSA-CMG2 is similar to those of sCMG2 and CMG2-Fc in in vitro toxin neutralization assays, and HSA-CMG2 completely protects rats from lethal doses of anthrax toxin challenge; these same challenge doses exceed sCMG2 at a sub-equivalent dose ratio and overwhelm CMG2-Fc. Our results suggest that HSA-CMG2 is a promising inhibitor of anthrax toxin and may contribute to the development of novel anthrax drugs.

Indexed as

Receptors, PeptideAnimalsAntigens, BacterialBacterial ToxinsCell LineEscherichia coliMaleMicePlasmidsRats, Inbred F344Rats, Sprague-DawleyRecombinant Fusion ProteinsSerum Albuminanthrax toxinAntigens, BacterialANTXR2 protein, humanBacterial ToxinsReceptors, PeptideRecombinant Fusion ProteinsSerum Albuminanthrax toxin inhibitorBacillus anthracisCMG2HSAprotective antigen

Identifiers

PMID26805881
PMCPMC4728550
OpenAlexW2270301109

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.