{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,13]],"date-time":"2026-01-13T09:06:26Z","timestamp":1768295186872,"version":"3.49.0"},"reference-count":44,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2007,7,1]],"date-time":"2007-07-01T00:00:00Z","timestamp":1183248000000},"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":["Infect Immun"],"published-print":{"date-parts":[[2007,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Poly-\n            <jats:italic>N<\/jats:italic>\n            -acetyl-glucosamine (PNAG) is a staphylococcal surface polysaccharide influencing biofilm formation that is also under investigation for its vaccine potential. Antibodies that bind to PNAG with either low (&lt;15%) or high (&gt;90%) levels of acetate are superior at opsonic and protective activity compared with antibodies that bind to PNAG with only high levels (&gt;70%) of acetate. PNAG is synthesized by four proteins encoded within the intercellular adhesin (\n            <jats:italic>ica<\/jats:italic>\n            ) locus\n            <jats:italic>icaADBC<\/jats:italic>\n            . In\n            <jats:italic>Staphylococcus epidermidis<\/jats:italic>\n            ,\n            <jats:italic>icaB<\/jats:italic>\n            encodes a deacetylase needed for the surface retention of PNAG and optimal biofilm formation. In this study, we confirmed that\n            <jats:italic>icaB<\/jats:italic>\n            plays a similar role in\n            <jats:italic>Staphylococcus aureus<\/jats:italic>\n            and found that an\n            <jats:italic>icaB<\/jats:italic>\n            mutant of\n            <jats:italic>S. aureus<\/jats:italic>\n            expressed significantly less surface-associated PNAG, was highly susceptible to antibody-independent opsonic killing that could not be enhanced with antibody raised against deacetylated PNAG (dPNAG), and had reduced survival capacity in a murine model of bacteremia. In contrast, an\n            <jats:italic>icaB<\/jats:italic>\n            -overexpressing strain produced primarily surface-associated PNAG, was more susceptible to opsonophagocytosis with antibody to dPNAG, and had increased survival in a murine bacteremia model. The highly acetylated secreted PNAG was more effective at blocking opsonic killing mediated by a human monoclonal antibody (mAb) to native PNAG than it was at blocking killing mediated by a human mAb to dPNAG, which by itself was a more effective opsonin. Retention of dPNAG on the surface of\n            <jats:italic>S. aureus<\/jats:italic>\n            is key to increased survival during bacteremia and also provides a molecular mechanism explaining the superior opsonic and protective activity of antibody to dPNAG.\n          <\/jats:p>","DOI":"10.1128\/iai.00078-07","type":"journal-article","created":{"date-parts":[[2007,5,1]],"date-time":"2007-05-01T00:51:24Z","timestamp":1177980684000},"page":"3406-3413","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":108,"title":["Molecular Basis for Preferential Protective Efficacy of Antibodies Directed to the Poorly Acetylated Form of Staphylococcal Poly-\n            <i>N<\/i>\n            -Acetyl-\u03b2-(1-6)-Glucosamine"],"prefix":"10.1128","volume":"75","author":[{"given":"Nuno","family":"Cerca","sequence":"first","affiliation":[{"name":"Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts"},{"name":"Institute for Biotechnology and Bioengineering, Center for Biological Engineering, Universidade do Minho, Braga, Portugal"}]},{"given":"Kimberly K.","family":"Jefferson","sequence":"additional","affiliation":[{"name":"Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts"},{"name":"Department of Microbiology and Immunology, Virginia Commonwealth University, Richmond, Virginia"}]},{"given":"Tomas","family":"Maira-Litra\u0301n","sequence":"additional","affiliation":[{"name":"Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts"}]},{"given":"Danielle B.","family":"Pier","sequence":"additional","affiliation":[{"name":"Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts"}]},{"given":"Casie","family":"Kelly-Quintos","sequence":"additional","affiliation":[{"name":"Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts"}]},{"given":"Donald A.","family":"Goldmann","sequence":"additional","affiliation":[{"name":"Children's Hospital, Harvard Medical School, Boston, Massachusetts"}]},{"given":"Joana","family":"Azeredo","sequence":"additional","affiliation":[{"name":"Institute for Biotechnology and Bioengineering, Center for Biological Engineering, Universidade do Minho, Braga, Portugal"}]},{"given":"Gerald B.","family":"Pier","sequence":"additional","affiliation":[{"name":"Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.186.14.4665-4684.2004"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.2174\/1566524054022567"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1472-765X.2004.01601.x"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.resmic.2005.01.007"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/jcm.22.6.996-1006.1985"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.67.10.5427-5433.1999"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.69.6.4079-4085.2001"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.73.3.1811-1819.2005"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0928-8244(02)00463-7"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.29.18586"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.64.1.277-282.1996"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1996.tb02548.x"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2958.2003.03482.x"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.49.6.2467-2473.2005"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.186.8.2449-2456.2004"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0008-6215(03)00045-4"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.186.24.8213-8220.2004"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1139\/m67-144"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.74.5.2742-2750.2006"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1086\/497604"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.micpath.2003.12.004"},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.73.10.6868-6876.2005"},{"key":"e_1_3_2_24_2","first-page":"209","year":"1993","unstructured":"Lee, J. 1993. 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