{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T08:10:11Z","timestamp":1772179811170,"version":"3.50.1"},"reference-count":36,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[2006,5,1]],"date-time":"2006-05-01T00:00:00Z","timestamp":1146441600000},"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":["Eukaryot Cell"],"published-print":{"date-parts":[[2006,5]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:italic>Entamoeba histolytica<\/jats:italic>\n            , which causes amebic dysentery and liver abscesses, is spread via chitin-walled cysts. The most abundant protein in the cyst wall of\n            <jats:italic>Entamoeba invadens<\/jats:italic>\n            , a model for amebic encystation, is a lectin called EiJacob1. EiJacob1 has five tandemly arrayed, six-Cys chitin-binding domains separated by low-complexity Ser- and Thr-rich spacers.\n            <jats:italic>E. histolytica<\/jats:italic>\n            also has numerous predicted Jessie lectins and chitinases, which contain a single, N-terminal eight-Cys chitin-binding domain. We hypothesized that\n            <jats:italic>E. invadens<\/jats:italic>\n            cyst walls are composed entirely of proteins with six-Cys or eight-Cys chitin-binding domains and that some of these proteins contain sugars.\n            <jats:italic>E. invadens<\/jats:italic>\n            genomic sequences predicted seven Jacob lectins, five Jessie lectins, and three chitinases. Reverse transcription-PCR analysis showed that mRNAs encoding Jacobs, Jessies, and chitinases are increased during\n            <jats:italic>E. invadens<\/jats:italic>\n            encystation, while mass spectrometry showed that the cyst wall is composed of an \u223c30:70 mix of Jacob lectins (cross-linking proteins) and Jessie and chitinase lectins (possible enzymes). Three Jacob lectins were cleaved prior to Lys at conserved sites (e.g., TPSVDK) in the Ser- and Thr-rich spacers between chitin-binding domains. A model peptide was cleaved at the same site by papain and\n            <jats:italic>E. invadens<\/jats:italic>\n            Cys proteases, suggesting that the latter cleave Jacob lectins in vivo. Some Jacob lectins had\n            <jats:italic>O<\/jats:italic>\n            -phosphodiester-linked carbohydrates, which were one to seven hexoses long and had deoxysugars at reducing ends. We concluded that the major protein components of the\n            <jats:italic>E. invadens<\/jats:italic>\n            cyst wall all contain chitin-binding domains (chitinases, Jessie lectins, and Jacob lectins) and that the Jacob lectins are differentially modified by site-specific Cys proteases and\n            <jats:italic>O<\/jats:italic>\n            -phosphodiester-linked glycans.\n          <\/jats:p>","DOI":"10.1128\/ec.5.5.836-848.2006","type":"journal-article","created":{"date-parts":[[2006,5,8]],"date-time":"2006-05-08T22:06:59Z","timestamp":1147126019000},"page":"836-848","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":40,"title":["Unique Posttranslational Modifications of Chitin-Binding Lectins of\n            <i>Entamoeba invadens<\/i>\n            Cyst Walls"],"prefix":"10.1128","volume":"5","author":[{"given":"Katrina L.","family":"Van Dellen","sequence":"first","affiliation":[{"name":"Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, Massachusetts 02118"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anirban","family":"Chatterjee","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, Massachusetts 02118"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel M.","family":"Ratner","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, Massachusetts 02118"},{"name":"Section of Infectious Diseases, Boston Medical Center, Boston, Massachusetts 02118"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paula E.","family":"Magnelli","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, Massachusetts 02118"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John F.","family":"Cipollo","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, Massachusetts 02118"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Martin","family":"Steffen","sequence":"additional","affiliation":[{"name":"Departments of Genetics and Genomics"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Phillips W.","family":"Robbins","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, Massachusetts 02118"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John","family":"Samuelson","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, Massachusetts 02118"},{"name":"Microbiology, Boston University School of Medicine, Boston, Massachusetts 02188"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/25.17.3389"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0404720101"},{"key":"e_1_3_2_4_2","first-page":"315","year":"1986","unstructured":"Bjerrum, O. J., and C. Schafer-Nielsen. 1986. Buffer systems and transfer parameters for semi-dry electroblotting with horizontal apparatus, p. 315-327. In J. J. Dunn (ed.), Electrophoresis '86. VCH, Weinheim, Germany.","journal-title":"Electrophoresis '86"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/EC.2.3.501-509.2003"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/0008-6215(84)85242-8"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0166-6851(96)02817-4"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1369-5274(00)00229-0"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1550-7408.2000.tb00083.x"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.68.7.4217-4224.2000"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJMra022710"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1002\/elps.200390069"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1089\/omi.2004.8.357"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.185.11.3352-3360.2003"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.2000.4315"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature03291"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.88.8.3248"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)45416-0"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.2000.3577"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1093\/protein\/12.1.3"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(77)90176-3"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0188-4409(00)00220-4"},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0409460102"},{"key":"e_1_3_2_24_2","doi-asserted-by":"publisher","DOI":"10.1006\/expr.1996.0092"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1021\/ac950914h"},{"key":"e_1_3_2_26_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0140-6736(03)12830-9"},{"key":"e_1_3_2_27_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0965-1748(98)00123-4"},{"key":"e_1_3_2_28_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/22.22.4673"},{"key":"e_1_3_2_29_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M110250200"},{"key":"e_1_3_2_30_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.70.6.3259-3263.2002"},{"key":"e_1_3_2_31_2","doi-asserted-by":"publisher","DOI":"10.2307\/3281741"},{"key":"e_1_3_2_32_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0166-6851(03)00073-2"},{"key":"e_1_3_2_33_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0074-7696(02)22016-1"},{"key":"e_1_3_2_34_2","first-page":"235","year":"2005","unstructured":"West, C. M., H. van der Wel, P. M. Coutinho, and B. Henrissat. 2005. Glycosyltransferase genomics in Dictyostelium, p. 235-264. In W. F. Loomis and A. Kuspa (ed.), Dictyostelium genomics. Horizon Bioscience, Norfolk, United Kingdom.","journal-title":"Dictyostelium genomics"},{"key":"e_1_3_2_35_2","doi-asserted-by":"publisher","DOI":"10.1007\/BF02100680"},{"key":"e_1_3_2_36_2","first-page":"553","volume":"112","year":"1999","unstructured":"Yates, J. R., III, E. Carmack, L. Hays, A. J. Link, and J. K. Eng. 1999. Automated protein identification using microcolumn liquid chromatography-tandem mass spectrometry. Methods Mol. Biol.112:553-569.","journal-title":"Methods Mol. Biol."},{"key":"e_1_3_2_37_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M500334200"}],"container-title":["Eukaryotic Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/EC.5.5.836-848.2006","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/EC.5.5.836-848.2006","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,2,23]],"date-time":"2022-02-23T14:10:05Z","timestamp":1645625405000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/EC.5.5.836-848.2006"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,5]]},"references-count":36,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2006,5]]}},"alternative-id":["10.1128\/EC.5.5.836-848.2006"],"URL":"https:\/\/doi.org\/10.1128\/ec.5.5.836-848.2006","relation":{},"ISSN":["1535-9778","1535-9786"],"issn-type":[{"value":"1535-9778","type":"print"},{"value":"1535-9786","type":"electronic"}],"subject":[],"published":{"date-parts":[[2006,5]]},"assertion":[{"value":"2006-01-17","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2006-03-03","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2006-05-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}