{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T02:54:21Z","timestamp":1792205661923,"version":"4.4.0"},"reference-count":38,"publisher":"American Society for Microbiology","issue":"23","license":[{"start":{"date-parts":[[2015,12,1]],"date-time":"2015-12-01T00:00:00Z","timestamp":1448928000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2015,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Bacillus anthracis<\/jats:named-content>\n            , a spore-forming pathogen, replicates as chains of vegetative cells by regulating the separation of septal peptidoglycan. Surface (S)-layer proteins and\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. anthracis<\/jats:named-content>\n            S-layer-associated proteins (BSLs) function as chain length determinants and are assembled in the envelope by binding to the secondary cell wall polysaccharide (SCWP).\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. anthracis<\/jats:named-content>\n            expresses six different genes encoding LytR-CpsA-Psr (LCP) enzymes (\n            <jats:italic>lcpB1<\/jats:italic>\n            to -\n            <jats:italic>4<\/jats:italic>\n            ,\n            <jats:italic>lcpC<\/jats:italic>\n            , and\n            <jats:italic>lcpD<\/jats:italic>\n            ), which when expressed in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Staphylococcus aureus<\/jats:named-content>\n            promote attachment of wall teichoic acid to peptidoglycan. Mutations in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. anthracis<\/jats:named-content>\n            <jats:italic>lcpB3<\/jats:italic>\n            and\n            <jats:italic>lcpD<\/jats:italic>\n            cause aberrations in cell size and chain length that can be explained as discrete defects in SCWP assembly; however, the function of the other\n            <jats:italic>lcp<\/jats:italic>\n            genes is not known. By deleting combinations of\n            <jats:italic>lcp<\/jats:italic>\n            genes from the\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. anthracis<\/jats:named-content>\n            genome, we generated variants with single\n            <jats:italic>lcp<\/jats:italic>\n            genes.\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. anthracis<\/jats:named-content>\n            expressing\n            <jats:italic>lcpB3<\/jats:italic>\n            alone displayed physiological cell size, vegetative growth, spore formation, and S-layer assembly. Strains expressing\n            <jats:italic>lcpB1<\/jats:italic>\n            or\n            <jats:italic>lcpB4<\/jats:italic>\n            displayed defects in cell size and shape, S-layer assembly, and spore formation yet sustained vegetative growth. In contrast, the\n            <jats:italic>lcpB2<\/jats:italic>\n            strain was unable to grow unless the gene was expressed from a multicopy plasmid (\n            <jats:italic>lcpB2<\/jats:italic>\n            <jats:sup>\n              <jats:italic>++<\/jats:italic>\n            <\/jats:sup>\n            ), and variants expressing\n            <jats:italic>lcpC<\/jats:italic>\n            or\n            <jats:italic>lcpD<\/jats:italic>\n            displayed severe defects in growth and cell shape. The\n            <jats:italic>lcpB2<\/jats:italic>\n            <jats:sup>\n              <jats:italic>++<\/jats:italic>\n            <\/jats:sup>\n            ,\n            <jats:italic>lcpC<\/jats:italic>\n            , or\n            <jats:italic>lcpD<\/jats:italic>\n            strains supported neither S-layer assembly nor spore formation. We propose a model whereby LCP enzymes fulfill partially overlapping functions in transferring SCWP molecules to discrete sites within the bacterial envelope.\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            Products of genes essential for bacterial envelope assembly represent targets for antibiotic development. The LytR-CpsA-Psr (LCP) enzymes tether bactoprenol-linked intermediates of secondary cell wall polymers to the C6 hydroxyl of\n            <jats:italic>N<\/jats:italic>\n            -acetylmuramic acid in peptidoglycan; however, the role of LCPs as a target for antibiotic therapy is not defined. We show here that LCP enzymes are essential for the cell cycle, vegetative growth, and spore formation of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Bacillus anthracis<\/jats:named-content>\n            , the causative agent of anthrax disease. Furthermore, we assign functions for each of the six LCP enzymes, including cell size and shape, vegetative growth and sporulation, and S-layer and S-layer-associated protein assembly.\n          <\/jats:p>","DOI":"10.1128\/jb.00656-15","type":"journal-article","created":{"date-parts":[[2015,9,22]],"date-time":"2015-09-22T02:23:48Z","timestamp":1442888628000},"page":"3731-3741","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":19,"title":["<i>Bacillus anthracis lcp<\/i>\n            Genes Support Vegetative Growth, Envelope Assembly, and Spore Formation"],"prefix":"10.1128","volume":"197","author":[{"given":"Megan","family":"Liszewski Zilla","sequence":"first","affiliation":[{"name":"Howard Taylor Ricketts Laboratory, Argonne National Laboratory, Lemont, Illinois, USA"},{"name":"Department of Microbiology, University of Chicago, Chicago, Illinois, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. 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