{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T18:13:23Z","timestamp":1791137603056,"version":"4.1.0"},"reference-count":56,"publisher":"American Society for Microbiology","issue":"6","license":[{"start":{"date-parts":[[2012,6,1]],"date-time":"2012-06-01T00:00:00Z","timestamp":1338508800000},"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":[[2012,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>Phagocytosis of host cells is characteristic of tissue invasion by the intestinal ameba<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Entamoeba histolytica<\/jats:named-content>, which causes amebic dysentery and liver abscesses.<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Entamoeba histolytica<\/jats:named-content>induces host cell apoptosis and uses ligands, including C1q, on apoptotic cells to engulf them. Two mass spectrometry analyses identified calreticulin in amebic phagosome preparations, and, in addition to its function as an endoplasmic reticulum chaperone, calreticulin is believed to be the macrophage receptor for C1q. The purpose of this study was to determine if calreticulin functions as an<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. histolytica<\/jats:named-content>C1q receptor during phagocytosis of host cells. Calreticulin was localized to the surface of<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. histolytica<\/jats:named-content>during interaction with both Jurkat lymphocytes and erythrocytes and was present in over 75% of phagocytic cups during amebic erythrophagocytosis. Presence of calreticulin on the cell surface was further demonstrated using a method that selectively biotinylated cell surface proteins and by flow cytometry using trophozoites overexpressing epitope-tagged calreticulin. Regulated overexpression of calreticulin increased<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. histolytica<\/jats:named-content>'s ability to phagocytose apoptotic lymphocytes and calcium ionophore-treated erythrocytes but had no effect on amebic adherence to or destruction of cell monolayers or surface expression of the GalNAc lectin and serine-rich<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. histolytica<\/jats:named-content>protein (SREHP) receptors. Finally,<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. histolytica<\/jats:named-content>calreticulin bound specifically to apoptotic lymphocytes and to human C1q. Collectively, these data implicate cell surface calreticulin as a receptor for C1q during<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. histolytica<\/jats:named-content>phagocytosis of host cells.<\/jats:p>","DOI":"10.1128\/iai.06287-11","type":"journal-article","created":{"date-parts":[[2012,4,3]],"date-time":"2012-04-03T04:59:56Z","timestamp":1333429196000},"page":"2008-2018","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":40,"title":["Entamoeba histolytica Cell Surface Calreticulin Binds Human C1q and Functions in Amebic Phagocytosis of Host Cells"],"prefix":"10.1128","volume":"80","author":[{"given":"Archana","family":"Vaithilingam","sequence":"first","affiliation":[{"name":"Cell and Molecular Biology Program, University of Vermont College of Medicine, Burlington, Vermont, USA"},{"name":"Department of Medicine, University of Vermont College of Medicine, Burlington, Vermont, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jose E.","family":"Teixeira","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Vermont College of Medicine, Burlington, Vermont, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter J.","family":"Miller","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Vermont College of Medicine, Burlington, Vermont, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bradley T.","family":"Heron","sequence":"additional","affiliation":[{"name":"Cell and Molecular Biology Program, University of Vermont College of Medicine, Burlington, Vermont, USA"},{"name":"Department of Medicine, University of Vermont College of Medicine, Burlington, Vermont, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher D.","family":"Huston","sequence":"additional","affiliation":[{"name":"Cell and Molecular Biology Program, University of Vermont College of Medicine, Burlington, Vermont, USA"},{"name":"Department of Medicine, University of Vermont College of Medicine, Burlington, Vermont, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.1998.00837.x"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.24.16917"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0166-6851(87)90150-2"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-1910(03)00025-8"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.162.2.546"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.58.7.2389-2391.1990"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1074-7613(01)00111-X"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0409219102"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.0040008"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.73.6.3422-3430.2005"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.36.1.396-406.1982"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.160.2.353"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.0020048"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0046-8177(70)80072-7"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijpara.2009.12.007"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molbiopara.2005.08.017"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/0035-9203(78)90144-X"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI200114122"},{"key":"e_1_3_2_20_2","doi-asserted-by":"crossref","first-page":"2207","DOI":"10.4049\/jimmunol.148.7.2207","article-title":"Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages","volume":"148","author":"Fadok VA","year":"1992","unstructured":"FadokVA. 1992. 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