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Signalization and cytoskeleton activity through myosin IB during the early steps of phagocytosis in Entamoeba histolytica: a proteomic approach
Open accessAbstract
Phagocytosis of human cells is a crucial activity for the virulence of the human parasite Entamoeba histolytica. This protozoan invades and destroys the intestine by killing and phagocytosing epithelial cells, erythrocytes and cells from the immune system. In this study, we used magnetic beads covered with proteins from human serum as a model system to study the early events involved in phagocytosis by E. histolytica. We validated the system showing that the beads uptake triggered the activation of the actin-myosin cytoskeleton and involved a PI3-kinase as previously described for erythrophagocytosis. We purified early phagosomes from wild-type (WT) amoeba and from parasites that overproduced myosin IB (MyoIB+), the unique unconventional myosin of E. histolytica. The MyoIB+ cells exhibit a slower and more synchronized uptake process than the WT strain. Proteomic analysis by liquid chromatography and tandem mass spectroscopy (LC-MS/MS) of the WT and MyoIB+ phagosomes allowed us to identify, for the first time, molecular actors involved in the early step of the uptake process. These include proteins involved in cytoskeleton activity, signalling, endocytosis, lytic activity and cell surface proteins. Interestingly, the proteins that we found specifically recruited on the phagosomes from the MyoIB+ strain were previously described in other eukarytotic cells, as involved in the regulation of cortical F-actin dynamics, such as alpha-actinin and formins. This proteomics approach allows a step further towards the understanding of the molecular mechanisms involved in phagocytosis in E. histolytica that revealed some interesting differences compared with phagocytosis in macrophages or Dictyostelium discoideum, and allowed to identify putative candidates for proteins linked to myosin IB activity during the phagocytic process.
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Metadata
- Authors
- Marion, S., Laurent, C., & Guillén, N.
- Affiliations
- Inserm (FR)
- Corresponding author
- Guillén, Nancy
- Venue
- Cellular Microbiology
- Publisher
- Wiley
- Published
- 2005-07-20
- Volume
- 7
- Issue
- 10
- Pages
- 1504-1518
- ISSN
- 1462-5814 (ISSN-L)
- OpenAlex
- W1590737147
- Cited by
- 125
- References
- 50
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 3 · 2023: 1 · 2022: 4 · 2021: 2 · 2020: 6 · 2019: 8 · 2018: 5 · 2017: 3 · 2016: 7 · 2015: 9 · 2014: 9 · 2013: 4 · 2012: 8
- FWCI
- 6.18
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cellular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Commission
- Fondation pour la Recherche Médicale
- Topics
- Health Sciences › Medicine › Infectious Diseases › Amoebic Infections and Treatments
- Life Sciences › Agricultural and Biological Sciences › Ecology, Evolution, Behavior and Systematics › Protist diversity and phylogeny
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- Entamoeba histolytica, phagocytosis, unconventional myosins, actin-myosin cytoskeleton, PI3-kinase, erythrophagocytosis, alpha-actinin, formins, signal transduction
- MeSH terms
- Actins, Animals, Chromatography, Liquid, Cytoskeleton, Dictyostelium, Entamoeba histolytica, Humans, Microscopy, Fluorescence, Phagocytosis, Phagosomes, Mass Spectrometry, Virulence, Signal Transduction, Genes, Protozoan, Proteome, Myosin Type I
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