Evidence map›Paper›PMID 39690153›Full record

ArticleNPJ vaccines2024

Immunogenic recombinant Mayaro virus-like particles present natively assembled glycoprotein.

Young Chan Kim, Yasunori Watanabe, Arlen-Celina Lücke, Xiyong Song, Raquel de Oliveira Souza, Robert Stass, Sasha R Azar, Shannan L Rossi, Carla Claser, Beate Mareike Kümmerer and 4 more

Erratum issuedAbstract read
In one paragraph

Article in NPJ vaccines, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. 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
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.

  1. Article
  2. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors.

Young Chan KimDepartment of Paediatrics, Oxford Vaccine Group, University of Oxford, Oxford, UK. young.kim@strubi.ox.ac.uk.
Yasunori WatanabeDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.
Arlen-Celina LückeInstitute of Virology, Medical Faculty, University of Bonn, Bonn, Germany.
Xiyong SongInstitute of Biotechnology, Helsinki Institute of Life Science HiLIFE, University of Helsinki, Helsinki, Finland.
Raquel de Oliveira SouzaDepartment of Parasitology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, SP, Brazil.
Robert StassDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.
Sasha R AzarDepartment of Pathology and the Institute for Human Infection and Immunity, University of Texas Medical Branch, Galveston, TX, USA.
Shannan L RossiDepartment of Pathology and the Institute for Human Infection and Immunity, University of Texas Medical Branch, Galveston, TX, USA.
Carla ClaserDepartment of Parasitology, Institute of Biomedical Sciences, University of São Paulo, São Paulo, SP, Brazil.
Beate Mareike KümmererInstitute of Virology, Medical Faculty, University of Bonn, Bonn, Germany.
Max CrispinSchool of Biological Sciences, University of Southampton, Southampton, UK.
Thomas A BowdenDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK.
Juha T HuiskonenInstitute of Biotechnology, Helsinki Institute of Life Science HiLIFE, University of Helsinki, Helsinki, Finland.
Arturo Reyes-SandovalInstituto Politécnico Nacional, IPN. Av. Luis Enrique Erro s/n. Unidad Adolfo López Mateos, Mexico City, Mexico.

Funding

Gates Foundation INV-008352Horizon 2020 734548Innovate UK 972212 and 971557International AIDS Vaccine Initiative INV-008352/OPP1153692Medical Research Council MR/S007555/1São Paulo Research Foundation (FAPESP) 2018/24470-0São Paulo Research Foundation (FAPESP) 2022/15124-6Wellcome TrustWellcome Trust 224117/Z/21/Z
6 · The paper itself

Abstract

Virus-like particles (VLPs) are an established vaccine platform and can be strong immunogens capable of eliciting both humoral and cellular immune responses against a range of pathogens. Here, we show by cryo-electron microscopy that VLPs of Mayaro virus, which contain envelope glycoproteins E1-E2 and capsid, exhibit an architecture that closely resembles native virus. In contrast to monomeric and soluble envelope 2 (E2) glycoprotein, both VLPs as well as the adenovirus and modified vaccinia virus Ankara (MVA) vaccine platforms expressing the equivalent envelope glycoproteins E1-E2, and capsid induced highly neutralising antibodies after immunisation. The levels of neutralising antibodies elicited by the viral-vectored vaccines of structural proteins and VLPs increased significantly upon boosting. Immunisation of Mayaro virus VLPs in mice with or without an adjuvant (poly:IC) yielded similar levels of neutralising antibodies suggesting that the VLPs may be used for immunisation without the need for an adjuvant. A single or two doses of non-adjuvanted 5 µg of MAYV VLP vaccination provided significant protection against viremia and MAYV-induced foot swelling in the C57BL/6 mouse challenge model. MAYV VLPs represent a non-infectious vaccine candidate, which may constitute a complementary option for future immunisation strategies against this important emerging alphavirus.

Identifiers

PMID39690153
PMCPMC11652679

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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.