{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T02:55:42Z","timestamp":1791341742644,"version":"4.3.1"},"reference-count":20,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[2009,6,1]],"date-time":"2009-06-01T00:00:00Z","timestamp":1243814400000},"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":[[2009,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Peptidoglycan is polymerized by monofunctional\n            <jats:sc>d<\/jats:sc>\n            ,\n            <jats:sc>d<\/jats:sc>\n            -transpeptidases belonging to class B penicillin-binding proteins (PBPs) and monofunctional glycosyltransferases and by bifunctional enzymes that combine both activities (class A PBPs). Three genes encoding putative class A PBPs (\n            <jats:italic>pbpF, pbpZ<\/jats:italic>\n            , and\n            <jats:italic>ponA<\/jats:italic>\n            ) were deleted from the chromosome of\n            <jats:italic>Enterococcus faecium<\/jats:italic>\n            D344R in all possible combinations in order to identify the glycosyltransferases that cooperate with low-affinity class B Pbp5 for synthesis of peptidoglycan in the presence of \u03b2-lactam antibiotics. The viability of the triple mutant indicated that glycan strands can be polymerized independently from class A PBPs by an unknown glycosyltranferase. The susceptibility of the \u0394\n            <jats:italic>pbpF<\/jats:italic>\n            \u0394\n            <jats:italic>ponA<\/jats:italic>\n            mutant and triple mutants to extended spectrum cephalosporins (ceftriaxone and cefepime) identified either PbpF or PonA as essential partners of Pbp5 for peptidoglycan polymerization in the presence of the drugs. Mass spectrometry analysis of peptidoglycan structure showed that loss of PonA and PbpF activity led to a minor decrease in the extent of peptidoglycan cross-linking by the remaining PBPs without any detectable compensatory increase in the participation of the\n            <jats:sc>l,d<\/jats:sc>\n            -transpeptidase in peptidoglycan synthesis. Optical density measurements and electron microscopy analyses showed that the \u0394\n            <jats:italic>pbpF<\/jats:italic>\n            \u0394\n            <jats:italic>ponA<\/jats:italic>\n            mutant underwent increased stationary-phase autolysis compared to the parental strain. Unexpectedly, deletion of the class A\n            <jats:italic>pbp<\/jats:italic>\n            genes revealed dissociation between the expression of resistance to cephalosporins and penicillins, although the production of Pbp5 was required for resistance to both classes of drugs. Thus, susceptibility of Pbp5-mediated peptidoglycan cross-linking to different \u03b2-lactam antibiotics differed as a function of its partner glycosyltransferase.\n          <\/jats:p>","DOI":"10.1128\/jb.01834-08","type":"journal-article","created":{"date-parts":[[2009,3,21]],"date-time":"2009-03-21T01:10:56Z","timestamp":1237597856000},"page":"3649-3656","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":67,"title":["Role of Class A Penicillin-Binding Proteins in the Expression of \u03b2-Lactam Resistance in\n            <i>Enterococcus faecium<\/i>"],"prefix":"10.1128","volume":"191","author":[{"given":"Louis B.","family":"Rice","sequence":"first","affiliation":[{"name":"Medical"},{"name":"Research"},{"name":"Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lenore L.","family":"Carias","sequence":"additional","affiliation":[{"name":"Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susan","family":"Rudin","sequence":"additional","affiliation":[{"name":"Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rebecca","family":"Hutton","sequence":"additional","affiliation":[{"name":"Research"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven","family":"Marshall","sequence":"additional","affiliation":[{"name":"Research"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Medhat","family":"Hassan","sequence":"additional","affiliation":[{"name":"Pathology and Laboratory Medicine Services, Louis Stokes Cleveland VA Medical Center"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nathalie","family":"Josseaume","sequence":"additional","affiliation":[{"name":"INSERM, U872, LRMA-Equipe 12, Paris, F-75006, France"},{"name":"Centre de Recherche des Cordeliers, Universite\u0301 Pierre et Marie Curie, UMR S 872, Paris F-75006, France"},{"name":"Universite\u0301 Paris Descartes, UMR S 872, Paris F-75006, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lionel","family":"Dubost","sequence":"additional","affiliation":[{"name":"Muse\u0301um National d'Histoire Naturelle, USM0502, Plateforme de Spectrome\u0301trie de Masse et de Prote\u0301omique du Muse\u0301um, De\u0301partement Recherche De\u0301veloppement et Diversite\u0301 Mole\u0301culaire, Paris F-75005, France"},{"name":"CNRS, UMR8041, Paris F-75005, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arul","family":"Marie","sequence":"additional","affiliation":[{"name":"Muse\u0301um National d'Histoire Naturelle, USM0502, Plateforme de Spectrome\u0301trie de Masse et de Prote\u0301omique du Muse\u0301um, De\u0301partement Recherche De\u0301veloppement et Diversite\u0301 Mole\u0301culaire, Paris F-75005, France"},{"name":"CNRS, UMR8041, Paris F-75005, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michel","family":"Arthur","sequence":"additional","affiliation":[{"name":"INSERM, U872, LRMA-Equipe 12, Paris, F-75006, France"},{"name":"Centre de Recherche des Cordeliers, Universite\u0301 Pierre et Marie Curie, UMR S 872, Paris F-75006, France"},{"name":"Universite\u0301 Paris Descartes, UMR S 872, Paris F-75006, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"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","unstructured":"Methods for dilutions antimicrobial susceptibility tests for bacteria that grow aerobically 2007"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.35.4.632"},{"key":"e_1_3_2_5_2","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/0147-619X(81)90035-4","volume":"6","year":"1981","unstructured":"Dunny, G., C. 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