Evidence map›Paper›PMID 25074930›Full record

ArticleThe Journal of biological chemistry2014

The merozoite surface protein 1 complex is a platform for binding to human erythrocytes by Plasmodium falciparum.

Clara S Lin, Alessandro D Uboldi, Danushka Marapana, Peter E Czabotar, Christian Epp, Hermann Bujard, Nicole L Taylor, Matthew A Perugini, Anthony N Hodder, Alan F Cowman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
7.1field-weighted citation impact, top 3% 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

32 citing papers in PubMed, 55 citations in OpenAlex.

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  11. Computational Clues of Immunogenic Hotspots inBioMed research international · 2022
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  16. Immunization with full-lengthNPJ vaccines · 2020
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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

10 authors at 4 institutions in 2 countries.

Clara S LinFrom the The Walter and Eliza Hall Institute of Medical Research, Melbourne 3052, Australia, Department of Medical Biology, The University of Melbourne, Melbourne 3010, Australia.
Alessandro D UboldiFrom the The Walter and Eliza Hall Institute of Medical Research, Melbourne 3052, Australia.
Danushka MarapanaFrom the The Walter and Eliza Hall Institute of Medical Research, Melbourne 3052, Australia, Department of Medical Biology, The University of Melbourne, Melbourne 3010, Australia.
Peter E CzabotarFrom the The Walter and Eliza Hall Institute of Medical Research, Melbourne 3052, Australia, Department of Medical Biology, The University of Melbourne, Melbourne 3010, Australia.
Christian EppDepartment of Infectious Diseases, Parasitology, Universität Heidelberg, INF 324, D-69120 Heidelberg, Germany.
Hermann BujardZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), INF 282, D-69120 Heidelberg, Germany, and.
Nicole L TaylorDepartment of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne 3082, Australia.
Matthew A PeruginiDepartment of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne 3082, Australia.
Anthony N HodderFrom the The Walter and Eliza Hall Institute of Medical Research, Melbourne 3052, Australia, Department of Medical Biology, The University of Melbourne, Melbourne 3010, Australia, hodder@wehi.edu.au.
Alan F CowmanFrom the The Walter and Eliza Hall Institute of Medical Research, Melbourne 3052, Australia, Department of Medical Biology, The University of Melbourne, Melbourne 3010, Australia, cowman@wehi.edu.au.
University of Melbourne · AUWalter and Eliza Hall Institute of Medical Research · AUHeidelberg University · DELa Trobe University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plasmodium falciparum is the causative agent of the most severe form of malaria in humans. The merozoite, an extracellular stage of the parasite lifecycle, invades erythrocytes in which they develop. The most abundant protein on the surface of merozoites is merozoite surface protein 1 (MSP1), which consists of four processed fragments. Studies indicate that MSP1 interacts with other peripheral merozoite surface proteins to form a large complex. Successful invasion of merozoites into host erythrocytes is dependent on this protein complex; however, the identity of all components and its function remain largely unknown. We have shown that the peripheral merozoite surface proteins MSPDBL1 and MSPDBL2 are part of the large MSP1 complex. Using surface plasmon resonance, we determined the binding affinities of MSPDBL1 and MSPDBL2 to MSP1 to be in the range of 2-4 × 10(-7) m. Both proteins bound to three of the four proteolytically cleaved fragments of MSP1 (p42, p38, and p83). In addition, MSPDBL1 and MSPDBL2, but not MSP1, bound directly to human erythrocytes. This demonstrates that the MSP1 complex acts as a platform for display of MSPDBL1 and MSPDBL2 on the merozoite surface for binding to receptors on the erythrocyte and invasion.

Indexed as

AnimalsErythrocytesHumansMalariaMembrane ProteinsMerozoitesMerozoite Surface Protein 1Multiprotein ComplexesPlasmodium falciparumProtein BindingProtozoan ProteinsMembrane ProteinsMerozoite Surface Protein 1Multiprotein ComplexesProtozoan ProteinsCell InvasionComplexfalciparumInfectionMalariaMerozoiteParasitePlasmodiumProtein Complex

Identifiers

PMID25074930
PMCPMC4162169
OpenAlexW2028406781

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.