Evidence map›Paper›PMID 26468747›Full record

ArticleCell host & microbe2015

Processing of Plasmodium falciparum Merozoite Surface Protein MSP1 Activates a Spectrin-Binding Function Enabling Parasite Egress from RBCs.

Sujaan Das, Nadine Hertrich, Abigail J Perrin, Chrislaine Withers-Martinez, Christine R Collins, Matthew L Jones, Jean M Watermeyer, Elmar T Fobes, Stephen R Martin, Helen R Saibil and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Cell host & microbe, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
16.9field-weighted citation impact, top 1% 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

113 citing papers in PubMed, 191 citations in OpenAlex.

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  17. The Plasmodium circumsporozoite protein.Trends in parasitology · 2024
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53 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 5 institutions in 2 countries.

Sujaan DasThe Francis Crick Institute, Mill Hill Laboratory, Mill Hill, London, NW7 1AA, UK.
Nadine HertrichDepartment für Infektiologie, Parasitologie, Universitätsklinikum Heidelberg, D-69120 Heidelberg, Germany.
Abigail J PerrinWellcome Trust Sanger Institute, Hinxton, Cambridge, CB10 1HH, UK.
Chrislaine Withers-MartinezThe Francis Crick Institute, Mill Hill Laboratory, Mill Hill, London, NW7 1AA, UK.
Christine R CollinsThe Francis Crick Institute, Mill Hill Laboratory, Mill Hill, London, NW7 1AA, UK.
Matthew L JonesThe Francis Crick Institute, Mill Hill Laboratory, Mill Hill, London, NW7 1AA, UK.
Jean M WatermeyerDepartment of Crystallography, Birkbeck College, London, WC1E 7HX, UK.
Elmar T FobesDepartment für Infektiologie, Parasitologie, Universitätsklinikum Heidelberg, D-69120 Heidelberg, Germany.
Stephen R MartinThe Francis Crick Institute, Mill Hill Laboratory, Mill Hill, London, NW7 1AA, UK.
Helen R SaibilDepartment of Crystallography, Birkbeck College, London, WC1E 7HX, UK.
Gavin J WrightWellcome Trust Sanger Institute, Hinxton, Cambridge, CB10 1HH, UK.
Moritz TreeckThe Francis Crick Institute, Mill Hill Laboratory, Mill Hill, London, NW7 1AA, UK.
Christian EppDepartment für Infektiologie, Parasitologie, Universitätsklinikum Heidelberg, D-69120 Heidelberg, Germany.
Michael J BlackmanThe Francis Crick Institute, Mill Hill Laboratory, Mill Hill, London, NW7 1AA, UK; Department of Pathogen Molecular Biology, London School of Hygiene and Tropical Medicine, London, WC1E 7HT, UK. Electronic address: mike.blackman@crick.ac.uk.
The Francis Crick Institute · GBHeidelberg University · DEBirkbeck, University of London · GBWellcome Sanger Institute · GBLondon School of Hygiene & Tropical Medicine · GB

Funding

Medical Research Council G1100013Medical Research Council MC_U117532063Medical Research Council MC_UP_1202/10Wellcome TrustWellcome Trust 098051
6 · The paper itself

Abstract

The malaria parasite Plasmodium falciparum replicates within erythrocytes, producing progeny merozoites that are released from infected cells via a poorly understood process called egress. The most abundant merozoite surface protein, MSP1, is synthesized as a large precursor that undergoes proteolytic maturation by the parasite protease SUB1 just prior to egress. The function of MSP1 and its processing are unknown. Here we show that SUB1-mediated processing of MSP1 is important for parasite viability. Processing modifies the secondary structure of MSP1 and activates its capacity to bind spectrin, a molecular scaffold protein that is the major component of the host erythrocyte cytoskeleton. Parasites expressing an inefficiently processed MSP1 mutant show delayed egress, and merozoites lacking surface-bound MSP1 display a severe egress defect. Our results indicate that interactions between SUB1-processed merozoite surface MSP1 and the spectrin network of the erythrocyte cytoskeleton facilitate host erythrocyte rupture to enable parasite egress.

Indexed as

Protein Processing, Post-TranslationalErythrocytesHost-Pathogen InteractionsHumansMerozoitesMerozoite Surface Protein 1Models, BiologicalPlasmodium falciparumProtein BindingProtein ConformationProteolysisProtozoan ProteinsSpectrinSubtilisinsMerozoite Surface Protein 1Protozoan ProteinsSpectrinSUB1 protein, Toxoplasma gondiiSubtilisins

Identifiers

PMID26468747
PMCPMC4608996
OpenAlexW2162684905

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.