Evidence map›Paper›PMID 38543863›Full record

ArticleVaccines2024

Vaccine Based on Recombinant Fusion Protein Combining Hepatitis B Virus PreS with SARS-CoV-2 Wild-Type- and Omicron-Derived Receptor Binding Domain Strongly Induces Omicron-Neutralizing Antibodies in a Murine Model.

Pia Gattinger, Bernhard Kratzer, Al Nasar Ahmed Sehgal, Anna Ohradanova-Repic, Laura Gebetsberger, Gabor Tajti, Margarete Focke-Tejkl, Mirjam Schaar, Verena Fuhrmann, Lukas Petrowitsch and 5 more

Open access · goldAbstract read
In one paragraph

Article in Vaccines, 2024. 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
0.8field-weighted citation impact, top 32% 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. 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 at 5 institutions in 2 countries.

Pia GattingerDivision of Immunopathology, Department of Pathophysiology and Allergy Research, Infectiology and Immunology, Center for Pathophysiology, Medical University of Vienna, 1090 Vienna, Austria.ORCID 0000-0001-6724-8543
Bernhard KratzerInstitute of Immunology, Infectiology and Immunology, Center for Pathophysiology, Medical University of Vienna, 1090 Vienna, Austria.ORCID 0000-0003-1091-4327
Al Nasar Ahmed SehgalInstitute of Immunology, Infectiology and Immunology, Center for Pathophysiology, Medical University of Vienna, 1090 Vienna, Austria.
Anna Ohradanova-RepicInstitute for Hygiene and Applied Immunology, Infectiology and Immunology, Center for Pathophysiology, Medical University of Vienna, 1090 Vienna, Austria.ORCID 0000-0002-8005-8522
Laura GebetsbergerInstitute for Hygiene and Applied Immunology, Infectiology and Immunology, Center for Pathophysiology, Medical University of Vienna, 1090 Vienna, Austria.
Gabor TajtiInstitute for Hygiene and Applied Immunology, Infectiology and Immunology, Center for Pathophysiology, Medical University of Vienna, 1090 Vienna, Austria.
Margarete Focke-TejklDivision of Immunopathology, Department of Pathophysiology and Allergy Research, Infectiology and Immunology, Center for Pathophysiology, Medical University of Vienna, 1090 Vienna, Austria.ORCID 0000-0003-3433-5071
Mirjam SchaarDivision of Immunopathology, Department of Pathophysiology and Allergy Research, Infectiology and Immunology, Center for Pathophysiology, Medical University of Vienna, 1090 Vienna, Austria.
Verena FuhrmannDivision of Immunopathology, Department of Pathophysiology and Allergy Research, Infectiology and Immunology, Center for Pathophysiology, Medical University of Vienna, 1090 Vienna, Austria.
Lukas PetrowitschInstitute of Molecular Biosciences, BioTechMed Graz, University of Graz, 8010 Graz, Austria.ORCID 0009-0001-7304-2231
Walter KellerInstitute of Molecular Biosciences, BioTechMed Graz, University of Graz, 8010 Graz, Austria.ORCID 0000-0002-2261-958X
Sandra HöglerUnit of Laboratory Animal Pathology, Institute of Pathology, University of Veterinary Medicine Vienna, 1210 Vienna, Austria.ORCID 0000-0002-6899-5273
Hannes StockingerInstitute for Hygiene and Applied Immunology, Infectiology and Immunology, Center for Pathophysiology, Medical University of Vienna, 1090 Vienna, Austria.ORCID 0000-0001-6404-4430
Winfried F PicklInstitute of Immunology, Infectiology and Immunology, Center for Pathophysiology, Medical University of Vienna, 1090 Vienna, Austria.
Rudolf ValentaDivision of Immunopathology, Department of Pathophysiology and Allergy Research, Infectiology and Immunology, Center for Pathophysiology, Medical University of Vienna, 1090 Vienna, Austria.
Medical University of Vienna · ATUniversity of Graz · ATKarl Landsteiner University of Health Sciences · ATSechenov University · RUUniversity of Veterinary Medicine Vienna · AT

Funding

FWF Austrian Science Fund P34253-BGovernment of Lower Austria Danube Allergy Research Cluster
6 · The paper itself

Abstract

backgroundCOVID-19, caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has become a recurrent endemic disease affecting the whole world. Since November 2021, Omicron and its subvariants have dominated in the spread of the disease. In order to prevent severe courses of disease, vaccines are needed to boost and maintain antibody levels capable of neutralizing Omicron. Recently, we produced and characterized a SARS-CoV-2 vaccine based on a recombinant fusion protein consisting of hepatitis B virus (HBV)-derived PreS and two SARS-CoV-2 wild-type RBDs.

objectivesTo develop a PreS-RBD vaccine which induces high levels of Omicron-specific neutralizing antibodies.

methodsWe designed, produced, characterized and compared strain-specific (wild-type: W-PreS-W; Omicron: O-PreS-O), bivalent (mix of W-PreS-W and O-PreS-O) and chimeric (i.e., W-PreS-O) SARS-CoV-2 protein subunit vaccines. Immunogens were characterized in vitro using protein chemical methods, mass spectrometry, and circular dichroism in combination with thermal denaturation and immunological methods. In addition, BALB/c mice were immunized with aluminum-hydroxide-adsorbed proteins and aluminum hydroxide alone (i.e., placebo) to study the specific antibody and cytokine responses, safety and Omicron neutralization.

resultsDefined and pure immunogens could be produced in significant quantities as secreted and folded proteins in mammalian cells. The antibodies induced after vaccination with different doses of strain-specific, bivalent and chimeric PreS-RBD fusion proteins reacted with wild-type and Omicron RBD in a dose-dependent manner and resulted in a mixed Th1/Th2 immune response. Interestingly, the RBD-specific IgG levels induced with the different vaccines were comparable, but the W-PreS-O-induced virus neutralization titers against Omicron (median VNT50: 5000) were seven- and twofold higher than the W-PreS-W- and O-PreS-O-specific ones, respectively, and they were six-fold higher than those of the bivalent vaccine.

conclusionAmong the tested immunogens, the chimeric PreS-RBD subunit vaccine, W-PreS-O, induced the highest neutralizing antibody titers against Omicron. Thus, W-PreS-O seems to be a highly promising COVID-19 vaccine candidate for further preclinical and clinical evaluation.

Indexed as

COVID-19neutralizing antibodiesOmicronSARS-CoV-2vaccine

Identifiers

PMID38543863
PMCPMC10975884
OpenAlexW4392110648

What Socratic 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 Socratic graph.