Evidence map›Paper›PMID 17468340›Full record

ArticleBlood2007

The ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasion.

Xinhong Pei, Xinhua Guo, Ross Coppel, Souvik Bhattacharjee, Kasturi Haldar, Walter Gratzer, Narla Mohandas, Xiuli An

Abstract read
In one paragraph

Article in Blood, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing 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

70 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
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  7. Article
  8. Review
  9. Article
  10. Article
  11. Identification of ExportedMicroorganisms · 2022
    Article
  12. Exported J domain proteins of the human malaria parasite.Frontiers in molecular biosciences · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

10 more citing papers are in PubMed but not listed here.

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

8 authors.

Xinhong PeiRed Cell Physiology Laboratory, New York Blood Center, 310 E. 67th Street, New York, NY 10021, USA.
Xinhua Guo
Ross Coppel
Souvik Bhattacharjee
Kasturi Haldar
Walter Gratzer
Narla Mohandas
Xiuli An

Funding

YEAST MEMBRANE CYTOSKELETONP01DK032094 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI NARLA, MOHANDAS · 1987 to 2021
$26.7M
Non-human primate models of malarial anemiaP01HL078826 · NHLBI · UNIVERSITY OF NOTRE DAME · PI HALDAR, KASTURI · 2005 to 2009
$6.9M
RED CELL DEFORMABILITY IN VITRO AND SURVIVAL IN VIVOR37DK026263 · NIDDK · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI NARLA, MOHANDAS · 1995 to 2017
$4.5M
RED CELL DEFORMABILITY IN VITRO AND SURVIVAL IN VIVOR01DK026263 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI NARLA, MOHANDAS · 1986 to 2007
$1.6M
NHLBI NIH HHS HL 78826NHLBI NIH HHS P01 HL078826NIDDK NIH HHS DK 26263NIDDK NIH HHS DK 32094NIDDK NIH HHS P01 DK032094NIDDK NIH HHS R01 DK026263NIDDK NIH HHS R37 DK026263
6 · The paper itself

Abstract

The malaria parasite Plasmodium falciparum releases the ring-infected erythrocyte surface antigen (RESA) inside the red cell on entry. The protein migrates to the host cell membrane, where it binds to spectrin, but neither the nature of the interaction nor its functional consequences have previously been defined. Here, we identify the binding motifs involved in the interaction and describe a possible function. We have found that spectrin binds to a 108-amino acid fragment (residues 663-770) of RESA, and that this RESA fragment binds to repeat 16 of the beta-chain, close to the labile dimer-dimer self-association site. We further show that the RESA fragment stabilizes the spectrin tetramer against dissociation into its constituent dimers, both in situ and in solution. This is accompanied by enhanced resistance of the cell to both mechanical and thermal degradation. Resealed erythrocytes containing RESA(663-770) display resistance to invasion by merozoites of P falciparum. We infer that the evolutionary advantage of RESA to the parasite lies in its ability to prevent invasion of cells that are already host to a developing parasite, as well as possibly to guard the cell against thermal damage at the elevated body temperatures prevailing in febrile crises.

Indexed as

Amino Acid MotifsAnimalsCells, CulturedErythrocyte MembraneHot TemperatureHumansPlasmodium falciparumProtein BindingProtein TransportProtozoan ProteinsRecombinant ProteinsSpectrinProtozoan ProteinsRecombinant Proteinsring-infected erythrocyte surface antigen (RESA), Plasmodium falciparumSpectrin

Identifiers

PMID17468340
PMCPMC1924765

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.