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In this study, we identified the<jats:named-content content-type=\"genus-species\">B. anthracis<\/jats:named-content><jats:italic>lcpD<\/jats:italic>mutant, which displays increased chain length and S-layer assembly defects due to diminished SCWP attachment to peptidoglycan. In contrast, the<jats:named-content content-type=\"genus-species\">B. anthracis<\/jats:named-content><jats:italic>lcpB3<\/jats:italic>variant displayed reduced cell size and chain length, which could be attributed to increased deposition of BSLs. In other bacteria, LytR-CpsA-Psr (LCP) proteins attach wall teichoic acid (WTA) and polysaccharide capsule to peptidoglycan.<jats:named-content content-type=\"genus-species\">B. anthracis<\/jats:named-content>does not synthesize these polymers, yet its genome encodes six LCP homologues, which, when expressed in<jats:named-content content-type=\"genus-species\">S. aureus<\/jats:named-content>, promote WTA attachment. We propose a model whereby<jats:named-content content-type=\"genus-species\">B. anthracis<\/jats:named-content>LCPs promote attachment of SCWP precursors to discrete locations in the peptidoglycan, enabling BSL assembly and regulated separation of septal peptidoglycan.<\/jats:p>","DOI":"10.1128\/jb.02364-14","type":"journal-article","created":{"date-parts":[[2014,11,11]],"date-time":"2014-11-11T05:10:25Z","timestamp":1415682625000},"page":"343-353","source":"Crossref","is-referenced-by-count":35,"title":["LytR-CpsA-Psr Enzymes as Determinants of Bacillus anthracis Secondary Cell Wall Polysaccharide Assembly"],"prefix":"10.1128","volume":"197","author":[{"given":"Megan","family":"Liszewski Zilla","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yvonne G. 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