{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,21]],"date-time":"2026-07-21T11:02:39Z","timestamp":1784631759713,"version":"3.55.0"},"reference-count":52,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2014,1,15]],"date-time":"2014-01-15T00:00:00Z","timestamp":1389744000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2014,2]]},"abstract":"Schistosomiasis is a major parasitic disease of humans, second only to malaria in its global impact. The disease is caused by digenean trematodes that infest the vasculature of their human hosts. These flukes are limited externally by a body wall composed of a syncytial epithelium, the apical surface membrane of which is a parasitism\u2010adapted dual membrane complex. Annexins are thought to be of integral importance for the stability of this apical membrane system. Here, we present the first structural and immunobiochemical characterization of an annexin from Schistosoma mansoni<\/jats:italic>. The crystal structure of annexin B22 confirms the presence of the previously predicted \u03b1\u2010helical segment in the II<\/jats:styled-content>\/III<\/jats:styled-content> linker and reveals a covalently linked head\u2010to\u2010head dimer. From the calcium\u2010bound crystal structure of this protein, canonical type II<\/jats:styled-content>, type III<\/jats:styled-content> and B site positions are occupied, and a novel binding site has been identified. The dimer arrangement observed in the crystal structure suggests the presence of two prominent features, a potential non\u2010canonical membrane binding site and a potential binding groove opposite to the former. Results from transcriptional profiling during development show that annexin B22 expression is correlated with life stages of the parasite that possess the syncytial tegument layer, and ultrastructural localization by immuno\u2010electron microscopy confirms the occurrence of annexins in the tegument of S. mansoni<\/jats:italic>. Data from membrane binding and aggregation assays indicate the presence of differential molecular mechanisms and support the hypothesis of annexin B22 providing structural integrity in the tegument.<\/jats:p><\/jats:sec>Database<\/jats:title>Coordinates and structure factors have been deposited with the PDB, accession numbers 4mdu<\/jats:ext-link>, 4mdv<\/jats:ext-link><\/jats:p><\/jats:sec>Structured digital abstract<\/jats:title>\n\n\nannexin B22<\/jats:ext-link> and annexin B22<\/jats:ext-link> bind<\/jats:ext-link> by molecular sieving<\/jats:ext-link> (View interaction<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n\nannexin B22<\/jats:ext-link>\u00a0and\u00a0annexin B22<\/jats:ext-link>\u00a0bind<\/jats:ext-link>\u00a0by\u00a0x-ray crystallography<\/jats:ext-link>\u00a0(View interaction<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n<\/jats:list>\n<\/jats:p><\/jats:sec>","DOI":"10.1111\/febs.12700","type":"journal-article","created":{"date-parts":[[2013,12,28]],"date-time":"2013-12-28T09:30:38Z","timestamp":1388223038000},"page":"1209-1225","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Crystal structure and immunological properties of the first annexin from Schistosoma\u00a0mansoni<\/i>: insights into the structural integrity of the schistosomal tegument"],"prefix":"10.1111","volume":"281","author":[{"given":"Chiuan Yee","family":"Leow","sequence":"first","affiliation":[{"name":"School of Veterinary Science University of Queensland Gatton Australia"},{"name":"Queensland Institute of Medical Research Herston Australia"},{"name":"Institute for Research in Molecular Medicine Universiti Sains Malaysia Penang Malaysia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charlene","family":"Willis","sequence":"additional","affiliation":[{"name":"Queensland Institute of Medical Research Herston Australia"},{"name":"Structural Chemistry Program Eskitis Institute Griffith University Brisbane Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Asiah","family":"Osman","sequence":"additional","affiliation":[{"name":"Structural Chemistry Program Eskitis Institute Griffith University Brisbane Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lyndel","family":"Mason","sequence":"additional","affiliation":[{"name":"Structural Chemistry Program Eskitis Institute Griffith University Brisbane Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anne","family":"Simon","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Lyon 1 Villeurbanne and Laboratoire Chimie et Biologie des Membranes et des Nanoobjets Universit\u00e9 Bordeaux Pessac France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian J.","family":"Smith","sequence":"additional","affiliation":[{"name":"La Trobe Institute for Molecular Science La Trobe University Melbourne Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robin B.","family":"Gasser","sequence":"additional","affiliation":[{"name":"Faculty of Veterinary Science University of Melbourne Parkville Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Malcolm K.","family":"Jones","sequence":"additional","affiliation":[{"name":"School of Veterinary Science University of Queensland Gatton Australia"},{"name":"Queensland Institute of Medical Research Herston Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andreas","family":"Hofmann","sequence":"additional","affiliation":[{"name":"Structural Chemistry Program Eskitis Institute Griffith University Brisbane 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