{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T12:58:22Z","timestamp":1790427502674,"version":"4.1.0"},"reference-count":24,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T00:00:00Z","timestamp":1789516800000},"content-version":"vor","delay-in-days":15,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Arch Insect Biochem Physiol"],"published-print":{"date-parts":[[2026,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    N\u2010glycosylation is an important regulator of insect development, tissue organization, neural function, and other physiological processes, yet the extent to which cultured insect cells reproduce organismal glycosylation remains poorly understood. Here, we characterized the whole\u2010body N\u2010glycoproteome of adult\n                    <jats:italic>Drosophila melanogaster<\/jats:italic>\n                    and compared it with our previously generated site\u2010specific glycoproteome of\n                    <jats:italic>Drosophila<\/jats:italic>\n                    S2 cells. Intact glycopeptide analysis by LC\u2010MS\/MS identified 2144 glycopeptides representing 526 glycoproteins, 875 N\u2010glycosylation sites, and 38 glycan compositions in adult flies. Both adult flies and S2 cells retained a broadly conserved glycan repertoire dominated by oligomannose\u2010type structures. However, this global similarity concealed substantial differences at the protein, site, and glycan levels. Only 34.6% of glycoproteins and 32.7% of glycosylation sites were shared between the two systems. Adult flies showed markedly higher representation of difucosylated glycans (12.0%\n                    <jats:italic>vs.<\/jats:italic>\n                    0.006% in S2 cells), including glycan structures associated with neural glycoproteins, and exhibited lower overall site\u2010specific microheterogeneity. At individual conserved sites, glycan processing could differ strikingly between systems, demonstrating that glycosylation is strongly influenced by organismal and cellular context. These findings establish a whole\u2010body adult\n                    <jats:italic>Drosophila<\/jats:italic>\n                    N\u2010glycoproteomic reference and show that S2 cells reproduce the core insect glycosylation program but only partially represent the protein\u2010 and site\u2010specific organization of glycosylation in the intact insect. The dataset provides a resource for investigating glycan\u2010dependent insect physiology and offers a useful benchmark for evaluating insect cell systems used in glycoprotein biotechnology.\n                  <\/jats:p>","DOI":"10.1002\/arch.70218","type":"journal-article","created":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T13:35:13Z","timestamp":1789565713000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Tissue Context Shapes N\u2010Glycan Processing and Site\u2010Specific Microheterogeneity in Adult\n                    <i>Drosophila melanogaster<\/i>\n                    Compared With S2 Cells"],"prefix":"10.1002","volume":"123","author":[{"ORCID":"https:\/\/orcid.org\/0009-0005-2299-4602","authenticated-orcid":false,"given":"Dongdong","family":"Liu","sequence":"first","affiliation":[{"name":"Institute of Entomology, Guizhou Key Laboratory of Agricultural Biosecurity Guizhou University Guiyang China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8334-3313","authenticated-orcid":false,"given":"Guy","family":"Smagghe","sequence":"additional","affiliation":[{"name":"Institute of Entomology, Guizhou Key Laboratory of Agricultural Biosecurity Guizhou University Guiyang China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,9,16]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M606711200"},{"key":"e_1_2_9_3_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M100573200"},{"key":"e_1_2_9_4_1","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/cwn096"},{"key":"e_1_2_9_5_1","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/cwm097"},{"key":"e_1_2_9_6_1","doi-asserted-by":"publisher","DOI":"10.1038\/nmeth.4256"},{"key":"e_1_2_9_7_1","doi-asserted-by":"publisher","DOI":"10.1002\/ps.6732"},{"key":"e_1_2_9_8_1","doi-asserted-by":"publisher","DOI":"10.1002\/ps.7145"},{"key":"e_1_2_9_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jinsphys.2019.03.009"},{"key":"e_1_2_9_10_1","article-title":"Site\u2010Resolved N\u2010Glycosylation Reveals Protein\u2010Specific Glycan Heterogeneity in Drosophila S2 Cells","author":"Liu D.","year":"2026","journal-title":"In Vitro Cellular and Developmental Biology\u2010Animal"},{"key":"e_1_2_9_11_1","doi-asserted-by":"publisher","DOI":"10.1021\/ac100530w"},{"key":"e_1_2_9_12_1","doi-asserted-by":"publisher","DOI":"10.1017\/S0031182019000398"},{"key":"e_1_2_9_13_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41592-020-0967-9"},{"key":"e_1_2_9_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.trac.2018.09.007"},{"issue":"1","key":"e_1_2_9_15_1","first-page":"7","article-title":"The Glycosylation Capacity of Insect Cells","volume":"81","author":"Rendi\u0107 D.","year":"2008","journal-title":"Croatica Chemica Acta"},{"key":"e_1_2_9_16_1","doi-asserted-by":"publisher","DOI":"10.1074\/mcp.RA119.001823"},{"key":"e_1_2_9_17_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.ibmb.2018.04.011"},{"key":"e_1_2_9_18_1","doi-asserted-by":"publisher","DOI":"10.1242\/dev.27.2.353"},{"key":"e_1_2_9_19_1","volume-title":"Essentials of Glycobiology","author":"Stanley 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Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/arch.70218","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/full-xml\/10.1002\/arch.70218","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/arch.70218","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T12:12:29Z","timestamp":1790424749000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/arch.70218"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9]]},"references-count":24,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2026,9]]}},"alternative-id":["10.1002\/arch.70218"],"URL":"https:\/\/doi.org\/10.1002\/arch.70218","archive":["Portico"],"relation":{},"ISSN":["0739-4462","1520-6327"],"issn-type":[{"value":"0739-4462","type":"print"},{"value":"1520-6327","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9]]},"assertion":[{"value":"2026-02-04","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication 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