Evidence map›Paper›PMID 34646979›Full record

ArticleAntibody therapeutics2021

Novel monkey mAbs induced by a therapeutic vaccine targeting the hepatitis B surface antigen effectively suppress hepatitis B virus in mice.

Yuanzhi Chen, Xinchu Xiang, Ruoyao Qi, Yiwen Wang, Yang Huang, Min You, Yangfei Xian, Yangtao Wu, Rao Fu, Ciming Kang and 6 more

Open access · goldAbstract read
In one paragraph

Article in Antibody therapeutics, 2021. 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
0.5field-weighted citation impact, top 35% 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, 3 citations in OpenAlex.

  1. Article
  2. 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

16 authors at 1 institution in 1 country.

Yuanzhi ChenState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Xinchu XiangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Ruoyao QiState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Yiwen WangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Yang HuangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Min YouState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Yangfei XianState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Yangtao WuState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Rao FuState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Ciming KangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Jixian TangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Hai YuState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Tianying ZhangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Quan YuanState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Wenxin LuoState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.
Ningshao XiaState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health and School of Life Science, Xiamen University, Xiamen 361102, China.ORCID 0000-0003-0179-5266
Xiamen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundWe have previously obtained a mouse anti-hepatitis B surface antigen (HBsAg) antibody E6F6 with long-lasting serum HBsAg clearance effects. The E6F6 epitope-based protein CR-T3-SEQ13 (HBsAg aa 113-135) vaccination therapy in cynomolgus monkeys induced long-term polyclonal antibodies-mediated clearance of HBsAg in the HBV transgenic (HBV-Tg) mice.

methodsWe isolated monoclonal antibodies from CR-T3-SEQ13 vaccinated cynomolgus monkeys, compared their therapeutic effects with E6F6, identified their epitopes on HBsAg, determined the pharmacokinetics and studied their physical property.

resultsA panel of anti-HBsAg mAbs was generated through memory B cell stimulatory culture. Two lead monkey-human chimeric antibodies, C1-23 and C3-23, effectively suppressed HBsAg and HBV DNA in HBV-Tg mice. The humanized antibodies and humanized-mouse reverse chimeric antibodies of two antibodies exhibited comparable HBsAg clearance and viral suppression efficacy as those versions of E6F6 in HBV-Tg mice. Humanized antibody hu1-23 exhibited more efficacy HBsAg-suppressing effects than huE6F6-1 and hu3-23 in HBV-Tg mice at dose levels of 10 and 20 mg/kg. Evaluation of the binding sites indicates that the epitope recognized by hu1-23 is located in HBsAg aa 118-125 and 121-125 for hu3-23. Physical property study revealed that hu1-23 and hu3-23 are stable enough for further development as a drug candidate.

conclusionsOur data suggest that the CR-T3-SEQ13 protein is a promising HBV therapeutic vaccine candidate, and hu1-23 and hu3-23 are therapeutic candidates for the treatment of chronic hepatitis b. Moreover, the generation of antibodies from the epitope-based vaccinated subjects may be an alternative approach for novel antibody drug discovery.

Indexed as

antibody-mediated HBV suppressionB cell culturechronic hepatitis B infectioncynomolgus monkey antibodyhepatitis B surface antigen

Identifiers

PMID34646979
PMCPMC8499627
OpenAlexW3201969001

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.