{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,8]],"date-time":"2026-01-08T03:53:46Z","timestamp":1767844426080,"version":"3.49.0"},"reference-count":28,"publisher":"Springer Science and Business Media LLC","issue":"4","license":[{"start":{"date-parts":[[2005,4,1]],"date-time":"2005-04-01T00:00:00Z","timestamp":1112313600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["www.embopress.org"],"crossmark-restriction":false},"short-container-title":["EMBO Reports"],"published-print":{"date-parts":[[2005,4]]},"abstract":"<jats:p>\n                    The\n                    <jats:italic>Drosophila<\/jats:italic>\n                    immune system is able to discriminate between classes of bacteria. Detection of Gram\u2010positive bacteria involves a complex of two pattern recognition receptors: peptidoglycan recognition protein SA (PGRP\u2010SA) and Gram\u2010negative binding protein 1 (GNBP1). These activate the Toll signalling pathway. To define the cell wall components sensed by the host, we used highly purified peptidoglycan fragments of two principal Gram\u2010positive bacterial pathogens\n                    <jats:italic>Staphylococcus aureus<\/jats:italic>\n                    and\n                    <jats:italic>Streptococcus pneumoniae<\/jats:italic>\n                    . We report that in both peptidoglycans, the minimal structure needed to activate the Toll pathway is a muropeptide dimer and that the free reducing end of the\n                    <jats:italic>N<\/jats:italic>\n                    \u2010acetyl muramic acid residues of the muropeptides is essential for activity. Monomeric muropeptides were inactive and inhibitory in combination with dimers. Finally, peptidoglycan was degraded by the haemolymph of wild\u2010type but not GNBP1 mutant flies. We suggest a model whereby GNBP1 is involved in the hydrolysis of Gram\u2010positive peptidoglycan producing new glycan reducing ends, which are subsequently detected by PGRP\u2010SA.\n                  <\/jats:p>","DOI":"10.1038\/sj.embor.7400371","type":"journal-article","created":{"date-parts":[[2005,3,24]],"date-time":"2005-03-24T12:12:35Z","timestamp":1111666355000},"page":"327-333","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":93,"title":["Requirements of peptidoglycan structure that allow detection by the\n                    <i>Drosophila<\/i>\n                    Toll pathway"],"prefix":"10.1038","volume":"6","author":[{"given":"Sergio R","family":"Filipe","sequence":"first","affiliation":[{"name":"Microbiology Unit, Department of Biochemistry, University of Oxford  South Parks Road Oxford OX1 3QU UK"},{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica\/Universidade Nova de Lisboa  Av. da Rep\u00fablica (EAN), Apartado 127 2781\u2010901 Oeiras Portugal"}]},{"given":"Alexander","family":"Tomasz","sequence":"additional","affiliation":[{"name":"The Rockefeller University  1230 York Avenue New York New York 10021 USA"}]},{"given":"Petros","family":"Ligoxygakis","sequence":"additional","affiliation":[{"name":"Genetics Unit, Department of Biochemistry, University of Oxford  South Parks Road Oxford OX1 3QU UK"}]}],"member":"297","published-online":{"date-parts":[[2005,4]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.93.13.6808"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1096-9888(199812)33:12<1182::AID-JMS733>3.0.CO;2-Q"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1056\/NEJMcibr040657"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1070216"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1002\/eji.200425095"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.C200651200"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1085432"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1038\/nature734"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1038\/nature02021"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1038\/ni0202-121"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0965-1748(98)00099-X"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/S1074-7613(04)00104-9"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1038\/35066006"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1038\/ni922"},{"key":"e_1_2_6_16_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.71.7.3707-3713.2003"},{"key":"e_1_2_6_17_1","doi-asserted-by":"publisher","DOI":"10.1038\/414756a"},{"key":"e_1_2_6_18_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.molimm.2003.10.008"},{"key":"e_1_2_6_19_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M313324200"},{"key":"e_1_2_6_20_1","doi-asserted-by":"publisher","DOI":"10.1038\/nature735"},{"key":"e_1_2_6_21_1","doi-asserted-by":"publisher","DOI":"10.1016\/S1074-7613(00)80208-3"},{"key":"e_1_2_6_22_1","doi-asserted-by":"publisher","DOI":"10.1038\/79801"},{"key":"e_1_2_6_23_1","doi-asserted-by":"publisher","DOI":"10.1128\/br.36.4.407-477.1972"},{"key":"e_1_2_6_24_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0891-5520(05)70082-9"},{"key":"e_1_2_6_25_1","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.173.12.7339"},{"key":"e_1_2_6_26_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0952-7915(03)00078-5"},{"key":"e_1_2_6_27_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.97.25.13772"},{"key":"e_1_2_6_28_1","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1119(90)90122-8"},{"key":"e_1_2_6_29_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M307475200"}],"container-title":["EMBO 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