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Morphodynamics of the Actin-Rich Cytoskeleton in Entamoeba histolytica

Overview of attention for article published in Frontiers in Cellular and Infection Microbiology, May 2018
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  • In the top 25% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (84th percentile)
  • High Attention Score compared to outputs of the same age and source (90th percentile)

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Title
Morphodynamics of the Actin-Rich Cytoskeleton in Entamoeba histolytica
Published in
Frontiers in Cellular and Infection Microbiology, May 2018
DOI 10.3389/fcimb.2018.00179
Pubmed ID
Authors

Maria Manich, Nora Hernandez-Cuevas, Juan D. Ospina-Villa, Sylvie Syan, Laurence A. Marchat, Jean-Christophe Olivo-Marin, Nancy Guillén

Abstract

Entamoeba histolytica is the anaerobic protozoan parasite responsible for human amoebiasis, the third most deadly parasitic disease worldwide. This highly motile eukaryotic cell invades human tissues and constitutes an excellent experimental model of cell motility and cell shape deformation. The absence of extranuclear microtubules in Entamoeba histolytica means that the actin-rich cytoskeleton takes on a crucial role in not only amoebic motility but also other processes sustaining pathogenesis, such as the phagocytosis of human cells and the parasite's resistance of host immune responses. Actin is highly conserved among eukaryotes, although diverse isoforms exist in almost all organisms studied to date. However, E. histolytica has a single actin protein, the structure of which differs significantly from those of its human homologs. Here, we studied the expression, structure and dynamics of actin in E. histolytica. We used molecular and cellular approaches to evaluate actin gene expression during intestinal invasion by E. histolytica trophozoites. Based on a three-dimensional structural bioinformatics analysis, we characterized protein domains differences between amoebic actin and human actin. Fine-tuned molecular dynamics simulations enabled us to examine protein motion and refine the three-dimensional structures of both actins, including elements potentially accounting for differences changes in the affinity properties of amoebic actin and deoxyribonuclease I. The dynamic, multifunctional nature of the amoebic cytoskeleton prompted us to examine the pleiotropic forms of actin structures within live E. histolytica cells; we observed the cortical cytoskeleton, stress fibers, "dot-like" structures, adhesion plates, and macropinosomes. In line with these data, a proteomics study of actin-binding proteins highlighted the Arp2/3 protein complex as a crucial element for the development of macropinosomes and adhesion plaques.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 48 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 48 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 9 19%
Student > Doctoral Student 5 10%
Student > Bachelor 4 8%
Professor 3 6%
Student > Master 3 6%
Other 6 13%
Unknown 18 38%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 16 33%
Agricultural and Biological Sciences 5 10%
Chemistry 2 4%
Mathematics 2 4%
Pharmacology, Toxicology and Pharmaceutical Science 1 2%
Other 2 4%
Unknown 20 42%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 13. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 07 April 2020.
All research outputs
#2,748,315
of 25,420,980 outputs
Outputs from Frontiers in Cellular and Infection Microbiology
#513
of 8,098 outputs
Outputs of similar age
#55,044
of 344,761 outputs
Outputs of similar age from Frontiers in Cellular and Infection Microbiology
#13
of 123 outputs
Altmetric has tracked 25,420,980 research outputs across all sources so far. Compared to these this one has done well and is in the 89th percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 8,098 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 5.8. This one has done particularly well, scoring higher than 93% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 344,761 tracked outputs that were published within six weeks on either side of this one in any source. This one has done well, scoring higher than 84% of its contemporaries.
We're also able to compare this research output to 123 others from the same source and published within six weeks on either side of this one. This one has done particularly well, scoring higher than 90% of its contemporaries.