Evidence map›Paper›PMID 31699037›Full record

ArticleBMC infectious diseases2019

Different mechanisms of two anti-anthrax protective antigen antibodies and function comparison between them.

Siping Xiong, Tingting Zhou, Feng Zheng, Xudong Liang, Yongping Cao, Chunhui Wang, Zhengqin Feng, Qi Tang, Jin Zhu

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC infectious diseases, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 89% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Targeting the Inside of Cells with Biologicals: Toxin Routes in a Therapeutic Context.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023
    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 4 institutions in 1 country.

Siping XiongEpidemiological Department, Huadong Medical Institute of Biotechniques, Nanjing, 210002, China.
Tingting ZhouEpidemiological Department, Huadong Medical Institute of Biotechniques, Nanjing, 210002, China.
Feng ZhengEpidemiological Department, Huadong Medical Institute of Biotechniques, Nanjing, 210002, China.
Xudong LiangNational Institute for Communicable Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing, 102206, China.
Yongping CaoEpidemiological Department, Huadong Medical Institute of Biotechniques, Nanjing, 210002, China.
Chunhui WangEpidemiological Department, Huadong Medical Institute of Biotechniques, Nanjing, 210002, China.
Zhengqin FengKey Laboratory of Antibody Technique of Ministry of Health, Nanjing Medical University, Nanjing, 210029, China.
Qi TangKey Laboratory of Antibody Technique of Ministry of Health, Nanjing Medical University, Nanjing, 210029, China. qitang@njmu.edu.cn.
Jin ZhuEpidemiological Department, Huadong Medical Institute of Biotechniques, Nanjing, 210002, China. zhujin1968@njmu.edu.cn.
Nanjing Medical University · CNHuadong Medical Institute of BiotechniquesHuadong Hospital · CNNational Institute for Communicable Disease Control and Prevention · CN

Funding

National Natural Science Foundation 31170884National Science and Technology Key Project on Major Infectious Diseases 2017ZX10303401, BWS17J034Science Fund of Jiangsu Province, China BE2018617
6 · The paper itself

Abstract

backgroundBacillus anthracis causes a highly lethal infectious disease primarily due to toxin-mediated injury. Antibiotics are no longer effective to treat the accumulation of anthrax toxin, thereby new strategies of antibody treatment are essential. Two anti- anthrax protective antigen (PA) antibodies, hmPA6 and PA21, have been reported by our lab previously.

methodsThe mechanisms of the two antibodies were elucidated by Electrophoresis, Competitive Enzyme-linked immune sorbent assay, Western blot analysis and immunoprecipitation test, and in vitro, in vivo (F344 rats) treatment test. The epitopes of the two antibodies were proved by Western blot and Enzyme-linked immune sorbent assay with different domains of PA.

resultsIn this study, we compared affinity and neutralization of these two antibodies. PA21 was better in protecting cells and rats, whereas hmPA6 had higher affinity. Furthermore, the neutralization mechanisms of the two antibodies and their recognition domains of PA were studied. The results showed that hmPA6 recognized domain IV, thus PA could not bind to cell receptors. Conversely, PA21 recognized domain II, thereby limiting heptamer oligomerization of PA63 in cells.

conclusionsOur studies elucidated the mechanisms and epitopes of hmPA6 and PA21. The present investigation can advance future use of the two antibodies in anthrax treatment or prophylaxis, and potentially as a combination treatment as the antibodies target different epitopes.

Indexed as

AnimalsAnthraxAntibodies, BacterialAntibodies, NeutralizingAntigens, BacterialBacillus anthracisBacterial ToxinsCell LineCell SurvivalElectrophoresisEpitopesImmunoassayRatsRats, Inbred F344anthrax toxinAntibodies, BacterialAntibodies, NeutralizingAntigens, BacterialBacterial ToxinsEpitopesAnthraxLethal toxinMechanismNeutralizing antibodyProtective antigen

Identifiers

PMID31699037
PMCPMC6836657
OpenAlexW2985040984

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.