Evidence map›Paper›PMID 26463341›Full record

ArticleMalaria journal2015

Immunogenicity and protective potential of a Plasmodium spp. enolase peptide displayed on archaeal gas vesicle nanoparticles.

Sneha Dutta, Priya DasSarma, Shiladitya DasSarma, Gotam K Jarori

Open access · goldAbstract read
In one paragraph

Article in Malaria journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. When Place Matters: Shuttling of Enolase-1 Across Cellular Compartments.Frontiers in cell and developmental biology · 2019
    Review
  7. Article
  8. Bionanotechnology for vaccine design.Current opinion in biotechnology · 2018
    Review
  9. Epitopes of Immunoreactive Proteins ofFrontiers in cellular and infection microbiology · 2018
    Article
  10. Serodiagnostic Potential of Alpha-Enolase FromFrontiers in microbiology · 2018
    Article
  11. Article
  12. Article
  13. 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

4 authors at 2 institutions in 2 countries.

Sneha DuttaDepartment of Biological Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai, 400005, India. snehadtt@yahoo.co.in.
Priya DasSarmaDepartment of Microbiology and Immunology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, MD, 21202, USA. pdassarma@som.umaryland.edu.
Shiladitya DasSarmaDepartment of Microbiology and Immunology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, MD, 21202, USA. sdassarma@som.umaryland.edu.
Gotam K JaroriDepartment of Biological Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai, 400005, India. GKJarori@gmail.com.
Tata Institute of Fundamental Research · INUniversity of Maryland, Baltimore · US

Funding

A Bioengineerable Self-adjuvating Nanoparticle for Antigen DeliveryR03AI107634 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI DASSARMA, SHILADITYA · 2013 to 2014
$154k
NIAID NIH HHS AI107634NIAID NIH HHS R03 AI107634
6 · The paper itself

Abstract

backgroundPlasmodium falciparum enolase has been shown to localize on the surface of merozoites and ookinetes. Immunization of mice with recombinant Plasmodium enolase (rPfeno) showed partial protection against malaria. Anti-rPfeno antibodies inhibited growth of the parasite in in vitro cultures and blocked ookinete invasion of mosquito midgut epithelium. It is hypothesized that parasite specific moonlighting functions (e.g. host cell invasion) may map on to unique structural elements of Pfeno. Since enolases are highly conserved between the host and the parasite, a parasite-specific epitope of enolase was displayed on novel protein nanoparticles produced by a halophilic Archaeon Halobacterium sp. NRC-1 and tested their ability to protect mice against live challenge.

methodsBy genetic engineering, a Plasmodium-enolase specific peptide sequence (104)EWGWS(108) with protective antigenic potential was inserted into the Halobacterium gas vesicle protein GvpC, a protein localized on the surface of immunogenic gas vesicle nanoparticles (GVNPs). Two groups of mice were immunized with the wild type (WT) and the insert containing recombinant (Rec) GVNPs respectively. A third group of mice was kept as un-immunized control. Antibody titres were measured against three antigens (i.e. WT-GVNPs, Rec-GVNPs and rPfeno) using ELISA. The protective potential was determined by measuring percentage parasitaemia and survival after challenge with the lethal strain Plasmodium yoelii 17XL.

resultsRec-GVNP-immunized mice showed higher antibody titres against rPfeno and Rec-GVNPs, indicating that the immunized mice had produced antibodies against the parasite enolase-specific insert sequence. Challenging the un-immunized, WT-GVNP and Rec-GVNP-immunized mice with a lethal strain of mice malarial parasite showed significantly lower parasitaemia and longer survival in the Rec-GVNP-immunized group as compared to control groups. The extent of survival advantage in the Rec-GVNP-group showed positive correlation with anti-rPfeno antibody titres while the parasitaemia showed a negative correlation. These results indicate that the parasite enolase peptide insert displayed on Halobacterium GVNPs is a good candidate as a protective antigenic epitope.

conclusionThe work reported here showed that the parasite-specific peptide sequence is a protective antigenic epitope. Although antibody response of B-cells to the guest sequence in Rec-GVNPs was mild, significant advantage in the control of parasitaemia and survival was observed. Future efforts are needed to display multiple antigens with protective properties to improve the performance of the GVNP-based approach.

Indexed as

AnimalsAntibodies, ProtozoanCytoplasmic VesiclesDisease Models, AnimalDrug CarriersEnzyme-Linked Immunosorbent AssayHalobacteriumMalariaMalaria VaccinesMaleMiceNanoparticlesParasitemiaPhosphopyruvate HydratasePlasmodiumProteinsAntibodies, ProtozoanDrug Carriersgas vesicle proteinMalaria VaccinesPhosphopyruvate HydrataseProteinsRecombinant ProteinsVaccines, Synthetic

Identifiers

PMID26463341
PMCPMC4605222
OpenAlexW1946666568

What OpenQuestion holds

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LicenceCC BY
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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.