{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T01:31:07Z","timestamp":1787016667814,"version":"build-2736575974"},"reference-count":48,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[2010,1,1]],"date-time":"2010-01-01T00:00:00Z","timestamp":1262304000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2010,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    <jats:italic>Entamoeba histolytica<\/jats:italic>\n                    is an intestinal protozoan parasite that causes amoebic dysentery and liver abscess. Phagocytosis by the parasite is a critical virulence process, since it is a prerequisite for tissue invasion and establishment of chronic infection. While the roles of many of the proteins that regulate phagocytosis-related signaling events in\n                    <jats:italic>E. histolytica<\/jats:italic>\n                    have been characterized, the functions of lipids in this cellular process remain largely unknown in this parasite. In other systems, phosphatidylinositol (3,4,5)-trisphosphate (PIP\n                    <jats:sub>3<\/jats:sub>\n                    ), a major product of phosphoinositide 3 kinase (PI3-kinase) activity, is essential for phagocytosis. Pleckstrin homology (PH) domains are protein domains that specifically bind to PIP\n                    <jats:sub>3<\/jats:sub>\n                    . In this study, we utilized glutathione\n                    <jats:italic>S<\/jats:italic>\n                    -transferase (GST)- and green fluorescent protein (GFP)-labeled PH domains as lipid biosensors to characterize the spatiotemporal aspects of PIP\n                    <jats:sub>3<\/jats:sub>\n                    distribution during various endocytic processes in\n                    <jats:italic>E. histolytica<\/jats:italic>\n                    . PIP\n                    <jats:sub>3<\/jats:sub>\n                    -specific biosensors accumulated at extending pseudopodia and in phagosomal cups in trophozoites exposed to erythrocytes but did not localize to pinocytic compartments during the uptake of a fluid-phase marker, dextran. Our results suggest that PIP\n                    <jats:sub>3<\/jats:sub>\n                    is involved in the early stages of phagosome formation in\n                    <jats:italic>E. histolytica<\/jats:italic>\n                    . In addition, we demonstrated that PIP\n                    <jats:sub>3<\/jats:sub>\n                    exists at high steady-state levels in the plasma membrane of\n                    <jats:italic>E. histolytica<\/jats:italic>\n                    and that these levels, unlike those in mammalian cells, are not abolished by serum withdrawal. Finally, expression of a PH domain in trophozoites inhibited erythrophagocytosis and enhanced motility, providing genetic evidence supporting the role of PI3-kinase signaling in these processes in\n                    <jats:italic>E. histolytica<\/jats:italic>\n                    .\n                  <\/jats:p>","DOI":"10.1128\/iai.00719-09","type":"journal-article","created":{"date-parts":[[2009,11,9]],"date-time":"2009-11-09T21:44:45Z","timestamp":1257803085000},"page":"125-137","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":33,"title":["Localization of Phosphatidylinositol (3,4,5)-Trisphosphate to Phagosomes in\n                    <i>Entamoeba histolytica<\/i>\n                    Achieved Using Glutathione\n                    <i>S<\/i>\n                    -Transferase- and Green Fluorescent Protein-Tagged Lipid Biosensors"],"prefix":"10.1128","volume":"78","author":[{"given":"Yevgeniya A.","family":"Byekova","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, Clemson University, Clemson, South Carolina 29634"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rhonda R.","family":"Powell","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Clemson University, Clemson, South Carolina 29634"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brenda H.","family":"Welter","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Clemson University, Clemson, South Carolina 29634"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lesly A.","family":"Temesvari","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Clemson University, Clemson, South Carolina 29634"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.135.5.1249"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cellbi.2004.01.005"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.160.2.353"},{"key":"e_1_3_2_5_2","first-page":"RA235","volume":"10","year":"2004","unstructured":"Chu, E. 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