{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T02:54:13Z","timestamp":1792032853879,"version":"4.4.0"},"reference-count":43,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2019,9,19]],"date-time":"2019-09-19T00:00:00Z","timestamp":1568851200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2019,11]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>The endospore of <jats:italic>Bacillus subtilis<\/jats:italic> is formed intracellularly upon nutrient starvation and is encased by proteinaceous shells. The outermost layer, the crust, is a postulated glycoprotein layer that is composed of six proteins: CotV, W, X, Y, Z and CgeA. Despite some insight into protein interactions and the identification of players in glycosylation, a clear picture of its architecture is still missing. Here, we report a comprehensive mutational analysis that confirms CotZ as the anchor of the crust, while the crust structure is provided by CotV, CotX and CotY. CotY seems to be the major structural component, while CotV and CotX are polar and co\u2010depend on each other and partially on CotW. CotW is independent of other crust proteins, instead depending on outer coat proteins, indicating a role at the interface of crust and coat. CgeA is co\u2010expressed with putative glycosyltransferases (CgeB and CgeD) and implicated in crust glycosylation. In accordance, we provide evidence that CgeB, CgeCDE, SpsA\u2010L, SpsM and SpsNOPQR (formerly YfnHGFED) contribute to the glycosylation state of the spore. The crust polysaccharide layer consists of functionally linked rhamnose\u2010 and galactose\u2010related variants and could contain rare sugars. It may therefore protect the crust against biological degradation and scavenging.<\/jats:p>","DOI":"10.1111\/mmi.14381","type":"journal-article","created":{"date-parts":[[2019,9,10]],"date-time":"2019-09-10T10:34:57Z","timestamp":1568111697000},"page":"1576-1592","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":40,"title":["The <i>Bacillus subtilis<\/i> endospore crust: protein interaction network, architecture and glycosylation state of a potential glycoprotein layer"],"prefix":"10.1111","volume":"112","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7145-7070","authenticated-orcid":false,"given":"Julia","family":"Bartels","sequence":"first","affiliation":[{"name":"Institute of Microbiology Technische Universit\u00e4t (TU) Dresden Dresden 01062 Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anja","family":"Bl\u00fcher","sequence":"additional","affiliation":[{"name":"School of Engineering Science 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