Evidence map›Paper›PMID 20083609›Full record

ArticleThe Journal of biological chemistry2010

Structure and function of a G-actin sequestering protein with a vital role in malaria oocyst development inside the mosquito vector.

Marion Hliscs, Julia M Sattler, Wolfram Tempel, Jennifer D Artz, Aiping Dong, Raymond Hui, Kai Matuschewski, Herwig Schüler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
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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

8 authors at 4 institutions in 3 countries.

Marion HliscsDepartment of Parasitology, Heidelberg University School of Medicine, 69120 Heidelberg, Germany.
Julia M Sattler
Wolfram Tempel
Jennifer D Artz
Aiping Dong
Raymond Hui
Kai Matuschewski
Herwig Schüler
Heidelberg University · DEStructural Genomics Consortium · CAUniversity of Toronto · CAKarolinska Institutet · SE

Funding

CIHRWellcome Trust
6 · The paper itself

Abstract

Cyclase-associated proteins (CAPs) are evolutionary conserved G-actin-binding proteins that regulate microfilament turnover. CAPs have a modular structure consisting of an N-terminal adenylate cyclase binding domain, a central proline-rich segment, and a C-terminal actin binding domain. Protozoan parasites of the phylum Apicomplexa, such as Cryptosporidium and the malaria parasite Plasmodium, express small CAP orthologs with homology to the C-terminal actin binding domain (C-CAP). Here, we demonstrate by reverse genetics that C-CAP is dispensable for the pathogenic Plasmodium blood stages. However, c-cap(-) parasites display a complete defect in oocyst development in the insect vector. By trans-species complementation we show that the Cryptosporidium parvum ortholog complements the Plasmodium gene functions. Purified recombinant C. parvum C-CAP protein binds actin monomers and prevents actin polymerization. The crystal structure of C. parvum C-CAP shows two monomers with a right-handed beta-helical fold intercalated at their C termini to form the putative physiological dimer. Our results reveal a specific vital role for an apicomplexan G-actin-binding protein during sporogony, the parasite replication phase that precedes formation of malaria transmission stages. This study also exemplifies how Plasmodium reverse genetics combined with biochemical and structural analyses of orthologous proteins can offer a fast track toward systematic gene characterization in apicomplexan parasites.

Indexed as

ActinsAmino Acid SequenceAnimalsCryptosporidium parvumCulicidaeHumansMalariaMicrofilament ProteinsModels, GeneticMolecular Sequence DataOocystsPhenotypePlasmodiumProtein BindingProtein Structure, TertiaryRecombinant ProteinsActinsMicrofilament ProteinsRecombinant Proteins

Identifiers

PMID20083609
PMCPMC2857035
OpenAlexW2004802638

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.