{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T02:54:32Z","timestamp":1792205672089,"version":"4.4.0"},"reference-count":67,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2005,6,15]],"date-time":"2005-06-15T00:00:00Z","timestamp":1118793600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2005,8]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Several examples of bacterial surface\u2010structure anchoring have been described, but they do not include polyglutamate capsule. <jats:italic>Bacillus anthracis<\/jats:italic> capsule, which is composed only of poly\u2010\u03b3\u2010 <jats:sc>d<\/jats:sc>\u2010glutamate, is one of the two major virulence factors of the bacterium. We analysed its anchoring. We report that the polyglutamate is anchored directly to the peptidoglycan and that the bond is covalent. We constructed a <jats:italic>capD<\/jats:italic> mutant strain, <jats:italic>capD<\/jats:italic> being the fourth gene of the capsule biosynthetic operon. The mutant bacilli are surrounded by polyglutamate material that is not covalently anchored. Thus, CapD is required for the covalent anchoring of polyglutamate to the peptidoglycan. Sequence similarities suggest that CapD is a \u03b3\u2010glutamyltranspeptidase. Furthermore, CapD is cleaved at the \u03b3\u2010glutamyltranspeptidase consensus cleavage site, and the two subunits remain associated, as necessary for \u03b3\u2010glutamyltranspeptidase activity. Other Gram\u2010positive \u03b3\u2010glutamyltranspeptidases are secreted, but CapD is located at the <jats:italic>Bacillus<\/jats:italic> surface, associated both with the membrane and the peptidoglycan. Polyglutamate is hydrolysed by CapD indicating that it is a CapD substrate. We suggest that CapD catalyses the capsule anchoring reaction. Interestingly, the CapD<jats:sup>\u2013<\/jats:sup> strain is far less virulent than the parental strain.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2005.04718.x","type":"journal-article","created":{"date-parts":[[2005,7,22]],"date-time":"2005-07-22T10:04:55Z","timestamp":1122026695000},"page":"717-726","source":"Crossref","is-referenced-by-count":157,"title":["<i>Bacillus anthracis<\/i> CapD, belonging to the \u03b3\u2010glutamyltranspeptidase family, is required for the covalent anchoring of capsule to peptidoglycan"],"prefix":"10.1111","volume":"57","author":[{"given":"Thomas","family":"Candela","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Agn\u00e8s","family":"Fouet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2005,6,30]]},"reference":[{"key":"e_1_2_6_2_1","first-page":"6003","article-title":"Physiological and biochemical characteristics of poly \u03b3\u2010glutamate synthetase complex of Bacillus subtilis. 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