Evidence map›Paper›PMID 16177378›Full record

ArticleInfection and immunity2005

Binding hot spot for invasion inhibitory molecules on Plasmodium falciparum apical membrane antigen 1.

Karen S Harris, Joanne L Casey, Andrew M Coley, Rosella Masciantonio, Jennifer K Sabo, David W Keizer, Erinna F Lee, Andrew McMahon, Raymond S Norton, Robin F Anders and 1 more

Abstract read
In one paragraph

Article in Infection and immunity, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

  1. Article
  2. The essential function of the apical polar ring during the blood stage ofbioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Conformational variability in the D2 loop ofJournal of structural biology: X · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Efficient refolding and functional characterization ofBiochemistry and biophysics reports · 2021
    Article
  12. Article
  13. Low-Complexity Repetitive Epitopes ofFrontiers in immunology · 2020
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
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.

Karen S HarrisDepartment of Biochemistry, La Trobe University, Victoria, Australia.
Joanne L Casey
Andrew M Coley
Rosella Masciantonio
Jennifer K Sabo
David W Keizer
Erinna F Lee
Andrew McMahon
Raymond S Norton
Robin F Anders
Michael Foley

Funding

Inhibitory epitopes in malaria vaccine candidatesR01AI059229 · NIAID · LA TROBE UNIVERSITY · PI FOLEY, MICHAEL · 2005 to 2009
$957k
NIAID NIH HHS R01 AI059229NIAID NIH HHS R01AI59229
6 · The paper itself

Abstract

Apical membrane antigen 1 (AMA1) is expressed in schizont-stage malaria parasites and sporozoites and is thought to be involved in the invasion of host red blood cells. AMA1 is an important vaccine candidate, as immunization with this antigen induces a protective immune response in rodent and monkey models of human malaria. Additionally, anti-AMA1 polyclonal and monoclonal antibodies inhibit parasite invasion in vitro. We have isolated a 20-residue peptide (R1) from a random peptide library that binds to native AMA1 as expressed by Plasmodium falciparum parasites. Binding of R1 peptide is dependent on AMA1 having the proper conformation, is strain specific, and results in the inhibition of merozoite invasion of host erythrocytes. The solution structure of R1, as determined by nuclear magnetic resonance spectroscopy, contains two structured regions, both involving turns, but the first region, encompassing residues 5 to 10, is hydrophobic and the second, at residues 13 to 17, is more polar. Several lines of evidence reveal that R1 targets a "hot spot" on the AMA1 surface that is also recognized by other peptides and monoclonal antibodies that have previously been shown to inhibit merozoite invasion. The functional consequence of binding to this region by a variety of molecules is the inhibition of merozoite invasion into host erythrocytes. The interaction between these peptides and AMA1 may further our understanding of the molecular mechanisms of invasion by identifying critical functional regions of AMA1 and aid in the development of novel antimalarial strategies.

Indexed as

Amino Acid SequenceAnimalsAntigens, ProtozoanAntimalarialsBiological AssayCarrier ProteinsMembrane ProteinsMolecular Sequence DataPeptide LibraryPlasmodium falciparumProtein ConformationProtozoan ProteinsAntigens, ProtozoanAntimalarialsapical membrane antigen I, PlasmodiumCarrier ProteinsMembrane ProteinsPeptide Librarypeptide R1Protozoan Proteins

Identifiers

PMID16177378
PMCPMC1230972

What OpenQuestion holds

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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.