{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T15:58:40Z","timestamp":1781107120838,"version":"3.54.1"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"8","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1991,4,15]]},"abstract":"<jats:p>Entamoeba histolytica trophozoites adhere to human colonic mucins and epithelial cells by a cell surface galactose-specific lectin. This lectin, which is composed of two subunits linked by disulfide bonds, has been shown to be a protective antigen in an animal model of amebiasis. We have determined the sequence of the mature form of the 170-kDa heavy subunit from cDNA clones and PCR-amplified fragments. The heavy subunit sequence consisted of a putative extracellular domain containing 1209 amino acids with 16 potential sites for N-linked glycosylation, a 26-amino acid hydrophobic region, and a 41-amino acid cytoplasmic tail. The presence of N-linked oligosaccharides was confirmed by culturing amebae with tunicamycin, which resulted in a decrease in the heavy subunit molecular mass to 160 kDa and a loss of lectin activity. The extracellular domain was remarkable for an extensive cysteine-rich domain that shared identify with similar regions of several other cell surface proteins and appeared to confer protease resistance to the subunit.<\/jats:p>","DOI":"10.1073\/pnas.88.8.3248","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T07:57:47Z","timestamp":1149062267000},"page":"3248-3252","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":109,"title":["Sequence of a cysteine-rich galactose-specific lectin of Entamoeba histolytica."],"prefix":"10.1073","volume":"88","author":[{"given":"B J","family":"Mann","sequence":"first","affiliation":[{"name":"Department of Medicine, University of Virginia, Charlottesville 22908."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B E","family":"Torian","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Virginia, Charlottesville 22908."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"T S","family":"Vedvick","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Virginia, Charlottesville 22908."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"suffix":"Jr","given":"W A","family":"Petri","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Virginia, Charlottesville 22908."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1991,4,15]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.88.8.3248","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T13:10:14Z","timestamp":1649855414000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.88.8.3248"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1991,4,15]]},"references-count":0,"journal-issue":{"issue":"8","published-print":{"date-parts":[[1991,4,15]]}},"alternative-id":["10.1073\/pnas.88.8.3248"],"URL":"https:\/\/doi.org\/10.1073\/pnas.88.8.3248","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1991,4,15]]},"assertion":[{"value":"1991-04-15","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}