Evidence map›Paper›PMID 22966050›Full record

ArticleInfection and immunity2012

Antigenic characterization of an intrinsically unstructured protein, Plasmodium falciparum merozoite surface protein 2.

Christopher G Adda, Christopher A MacRaild, Linda Reiling, Kaye Wycherley, Michelle J Boyle, Vivian Kienzle, Paul Masendycz, Michael Foley, James G Beeson, Raymond S Norton and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  4. Development of high affinity antibodies toFrontiers in immunology · 2025
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  8. Naturally acquired IgG responses toFrontiers in immunology · 2024
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  12. Review
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  14. Conformational diversity facilitates antibody mutation trajectories and discrimination between foreign and self-antigens.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Disordered epitopes as peptide vaccines.Peptide science (Hoboken, N.J.) · 2018
    Review
  19. Article
  20. 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

11 authors at 4 institutions in 1 country.

Christopher G AddaDepartment of Biochemistry, La Trobe University, Victoria, Australia.
Christopher A MacRaild
Linda Reiling
Kaye Wycherley
Michelle J Boyle
Vivian Kienzle
Paul Masendycz
Michael Foley
James G Beeson
Raymond S Norton
Robin F Anders
La Trobe University · AUBurnet Institute · AUMonash University · AUWalter and Eliza Hall Institute of Medical Research · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Merozoite surface protein 2 (MSP2) is an abundant glycosylphosphatidylinositol (GPI)-anchored protein of Plasmodium falciparum, which is a potential component of a malaria vaccine. As all forms of MSP2 can be categorized into two allelic families, a vaccine containing two representative forms of MSP2 may overcome the problem of diversity in this highly polymorphic protein. Monomeric recombinant MSP2 is an intrinsically unstructured protein, but its conformational properties on the merozoite surface are unknown. This question is addressed here by analyzing the 3D7 and FC27 forms of recombinant and parasite MSP2 using a panel of monoclonal antibodies raised against recombinant MSP2. The epitopes of all antibodies, mapped using both a peptide array and by nuclear magnetic resonance (NMR) spectroscopy on full-length recombinant MSP2, were shown to be linear. The antibodies revealed antigenic differences, which indicate that the conserved N- and C-terminal regions, but not the central variable region, are less accessible in the parasite antigen. This appears to be an intrinsic property of parasite MSP2 and is not dependent on interactions with other merozoite surface proteins as the loss of some conserved-region epitopes seen using the immunofluorescence assay (IFA) on parasite smears was also seen on Western blot analyses of parasite lysates. Further studies of the structural basis of these antigenic differences are required in order to optimize recombinant MSP2 constructs being evaluated as potential vaccine components.

Indexed as

Epitope MappingAnimalsAntibodies, MonoclonalAntigens, ProtozoanFemaleMagnetic Resonance SpectroscopyMiceMice, Inbred CBAPlasmodium falciparumProtein ConformationProtozoan ProteinsRecombinant ProteinsAntibodies, MonoclonalAntigens, Protozoanmerozoite surface protein 2, PlasmodiumProtozoan ProteinsRecombinant Proteins

Identifiers

PMID22966050
PMCPMC3497424
OpenAlexW2105399619

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.