Abstract |
The unicellular parasite Entamoeba histolytica, the causative agent of the human disease amebiasis, has traditionally been distinguished from its nonpathogenic cousin Entamoeba dispar by its propensity for the ingestion of erythrocytes. This classic feature, along with the parasite's ability to cause extensive host cell death, are critical mechanisms of pathogenesis during human infection. Recent advances have led to a greater understanding of the molecular components that allow E. histolytica to kill and phagocytose extracellular targets during human infection and include detailed studies of the role of the parasite's cysteine proteinases and other effectors of cytotoxicity, as well as the mechanisms of ligand recognition, signaling and intracellular trafficking during phagocytosis.
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Authors | Nathaniel C V Christy, William A Petri Jr |
Journal | Future microbiology
(Future Microbiol)
Vol. 6
Issue 12
Pg. 1501-19
(Dec 2011)
ISSN: 1746-0921 [Electronic] England |
PMID | 22122445
(Publication Type: Journal Article, Research Support, N.I.H., Extramural, Review)
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Chemical References |
- Virulence Factors
- Cysteine Proteases
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Topics |
- Cell Adhesion
- Cysteine Proteases
(metabolism)
- Entamoeba histolytica
(enzymology, immunology, pathogenicity)
- Humans
- Models, Biological
- Phagocytosis
- Virulence Factors
(metabolism)
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