Evidence map›Paper›PMID 37342672›Full record

ArticleInnovation (Cambridge (Mass.))2023

Precise modification of the surface charge of antigen enhances vaccine immunogenicity.

Xiaodong Zai, Zhiling Zhang, Chuge Zhou, Fangxin Zhao, Yue Zhang, Xiaolin Wang, Ruihua Li, Yaohui Li, Xiaofan Zhao, Shuyi Wang and 5 more

Abstract read
In one paragraph

Article in Innovation (Cambridge (Mass.)), 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
–field-weighted citation impact
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.

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

15 authors.

Xiaodong ZaiInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.
Zhiling ZhangCollege of pharmacy, Nanjing University of Chinese Medicine, Nanjing 210023, China.
Chuge ZhouInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.
Fangxin ZhaoInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.
Yue ZhangInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.
Xiaolin WangInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.
Ruihua LiInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.
Yaohui LiInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.
Xiaofan ZhaoInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.
Shuyi WangInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.
Yilong YangInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.
Ying YinInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.
Jun ZhangInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.
Junjie XuInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.
Wei ChenInstitute of Biotechnology, Academy of Military Medical Sciences, Beijing 100071, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aluminum (alum) adjuvant is the most extensively used protein subunit vaccine adjuvant, and its effectiveness and safety have been widely recognized. The surface charge of the antigen determines its electrostatic adsorption to alum adjuvant, which directly affects the immune efficacy of the protein vaccine. In our study, we precisely modified its surface charge by inserting charged amino acids into the flexible region of the SARS-CoV-2 receptor-binding domain (RBD), achieving electrostatic adsorption and a site-specific anchor between the immunogen and alum adjuvant. This innovative strategy extended the bioavailability of the RBD and directionally displayed the neutralizing epitopes, thereby significantly enhancing humoral and cellular immunity. Furthermore, the required dose of antigen and alum adjuvant was greatly reduced, which improved the safety and accessibility of the protein subunit vaccine. On this basis, the wide applicability of this novel strategy to a series of representative pathogen antigens such as SARS-RBD, MERS-RBD, Mpox-M1, MenB-fHbp, and Tularemia-Tul4 was further confirmed. Charge modification of antigens provides a straightforward approach for antigenicity optimization of alum-adjuvanted vaccines, which has great potential to be adopted as a global defense against infectious diseases.

Identifiers

PMID37342672
PMCPMC10277596

What OpenQuestion holds

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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.