{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T02:24:14Z","timestamp":1772159054388,"version":"3.50.1"},"reference-count":38,"publisher":"American Society for Microbiology","issue":"10","license":[{"start":{"date-parts":[[2011,5,15]],"date-time":"2011-05-15T00:00:00Z","timestamp":1305417600000},"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":[[2011,5,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The polymerization of peptidoglycan is the result of two types of enzymatic activities: transglycosylation, the formation of linear glycan chains, and transpeptidation, the formation of peptide cross-bridges between the glycan strands.\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            has four penicillin binding proteins (PBP1 to PBP4) with transpeptidation activity, one of which, PBP2, is a bifunctional enzyme that is also capable of catalyzing transglycosylation reactions. Additionally, two monofunctional transglycosylases have been reported in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">S. aureus<\/jats:named-content>\n            : MGT, which has been shown to have\n            <jats:italic>in vitro<\/jats:italic>\n            transglycosylase activity, and a second putative transglycosylase, SgtA, identified only by sequence analysis. We have now shown that purified SgtA has\n            <jats:italic>in vitro<\/jats:italic>\n            transglycosylase activity and that both MGT and SgtA are not essential in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">S. aureus.<\/jats:named-content>\n            However, in the absence of PBP2 transglycosylase activity, MGT but not SgtA becomes essential for cell viability. This indicates that\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">S. aureus<\/jats:named-content>\n            cells require one transglycosylase for survival, either PBP2 or MGT, both of which can act as the sole synthetic transglycosylase for cell wall synthesis. We have also shown that both MGT and SgtA interact with PBP2 and other enzymes involved in cell wall synthesis in a bacterial two-hybrid assay, suggesting that these enzymes may work in collaboration as part of a larger, as-yet-uncharacterized cell wall-synthetic complex.\n          <\/jats:p>","DOI":"10.1128\/jb.01474-10","type":"journal-article","created":{"date-parts":[[2011,3,27]],"date-time":"2011-03-27T00:13:53Z","timestamp":1301184833000},"page":"2549-2556","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":53,"title":["Monofunctional Transglycosylases Are Not Essential for Staphylococcus aureus Cell Wall Synthesis"],"prefix":"10.1128","volume":"193","author":[{"given":"Patricia","family":"Reed","sequence":"first","affiliation":[{"name":"Laboratory of Bacterial Cell Biology, Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Avenida da Rep\u00fablica, 2781-901 Oeiras, Portugal"}]},{"given":"Helena","family":"Veiga","sequence":"additional","affiliation":[{"name":"Laboratory of Bacterial Cell Biology, Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Avenida da Rep\u00fablica, 2781-901 Oeiras, Portugal"}]},{"given":"Ana M.","family":"Jorge","sequence":"additional","affiliation":[{"name":"Laboratory of Bacterial Cell Biology, Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Avenida da Rep\u00fablica, 2781-901 Oeiras, Portugal"}]},{"given":"Mohammed","family":"Terrak","sequence":"additional","affiliation":[{"name":"Centre d'Ing\u00e9nierie des Prot\u00e9ines, Universit\u00e9 de Li\u00e8ge, Institut de Chimie, B6a Sart-Tilman, 4000 Li\u00e8ge, Belgium"}]},{"given":"Mariana G.","family":"Pinho","sequence":"additional","affiliation":[{"name":"Laboratory of Bacterial Cell Biology, Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Avenida da Rep\u00fablica, 2781-901 Oeiras, Portugal"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.186.5.1221-1228.2004"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.70.11.6887-6891.2004"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1004304107"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.187.6.2215-2217.2005"},{"key":"e_1_3_2_6_2","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.micpath.2004.07.004","article-title":"The role of integrase\/recombinase xerD and monofunctional biosynthesis peptidoglycan transglycosylase genes in pathogenicity of Brucella abortus infection in vitro and in vivo","volume":"37","author":"Canavessi A. 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