Evidence map›Paper›PMID 39815669›Full record

ArticleFEBS open bio2025

Expression and purification of E140 protein antigen fragments of Plasmodium vivax and Plasmodium berghei for serological assays.

Rodolfo Ferreira Marques, Edit Ábrahám, Hiromi Muramatsu, Daniel Youssef Bargieri, Norbert Pardi, Zoltán Lipinszki

Abstract read
In one paragraph

Article in FEBS open bio, 2025. 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
–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

1 citing paper in PubMed.

  1. An mRNA-lipid nanoparticle vaccine targeting theMolecular therapy. Nucleic acids · 2026
    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

6 authors.

Rodolfo Ferreira MarquesDepartment of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.
Edit ÁbrahámSynthetic and Systems Biology Unit, Institute of Biochemistry, HUN-REN Biological Research Centre, Szeged, Hungary.ORCID https://orcid.org/0000-0002-1268-760X
Hiromi MuramatsuDepartment of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID https://orcid.org/0000-0003-1544-1493
Daniel Youssef BargieriDepartment of Parasitology, Institute of Biomedical Sciences, University of Sao Paulo, São Paulo, Brazil.
Norbert PardiDepartment of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.
Zoltán LipinszkiSynthetic and Systems Biology Unit, Institute of Biochemistry, HUN-REN Biological Research Centre, Szeged, Hungary.ORCID https://orcid.org/0000-0002-2067-0832

Funding

Fundação de Amparo à Pesquisa do Estado de São Paulo FAPESP 2021/06769-0Fundação de Amparo à Pesquisa do Estado de São Paulo FAPESP 2022/15895-2Magyar Tudományos Akadémia Lendület Program Grant (LP2017-7/2017)National Institute of Allergy and Infectious Diseases R01AI146101National Institute of Allergy and Infectious Diseases R01AI153064National Research, Development and Innovation Office 2022-2.1.1-NL-2022-00008Nemzeti Kutatási Fejlesztési és Innovációs Hivatal 2021-1.1.4-GYORSÍTÓSÁV-2022-00008
6 · The paper itself

Abstract

Malaria, a life-threatening disease caused by Plasmodium parasites, continues to pose a significant global health threat, with nearly 250 million infections and over 600 000 deaths reported annually by the WHO. Fighting malaria is particularly challenging partly due to the complex life cycle of the parasite. However, technological breakthroughs such as the development of the nucleoside-modified mRNA lipid nanoparticle (mRNA-LNP) vaccine platform, along with the discovery of novel conserved Plasmodium antigens such as the E140 protein, present new opportunities in malaria prevention. Importantly, production of recombinant proteins for malaria vaccine evaluation by serological assays often represents an additional hurdle because many Plasmodium proteins are complex and often contain transmembrane domains that make production and purification particularly difficult. This research protocol provides a step-by-step guide for the production and purification of P. berghei and P. vivax E140 protein fragments that can be used to test humoral immune responses against this novel malaria vaccine target. We demonstrate that the purified proteins can be successfully used in enzyme-linked immunosorbent assay (ELISA) to evaluate antigen-specific binding antibody responses in sera obtained from E140 mRNA-LNP-vaccinated mice. Therefore, these proteins can contribute to the development and evaluation of E140-based malaria vaccines.

Indexed as

Antigens, ProtozoanPlasmodium bergheiPlasmodium vivaxProtozoan ProteinsAnimalsAntibodies, ProtozoanEnzyme-Linked Immunosorbent AssayFemaleHumansMalariaMalaria VaccinesMiceMice, Inbred BALB CRecombinant ProteinsSerologic TestsAntibodies, ProtozoanAntigens, ProtozoanMalaria VaccinesProtozoan ProteinsRecombinant ProteinsELISAMalariamRNA‐lipid nanoparticlePlasmodium spp.protein purificationrecombinant E140 fragmentsserological assaysvaccine development

Identifiers

PMID39815669
PMCPMC12051032

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Registered trials

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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.