{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"bioRxiv"}],"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T19:13:42Z","timestamp":1768504422658,"version":"3.49.0"},"posted":{"date-parts":[[2023,5,31]]},"group-title":"Neuroscience","reference-count":25,"publisher":"openRxiv","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2023,5,30]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                <jats:p>Protein N-linked glycosylation is a ubiquitous modification in the secretory pathway that plays a critical role in the development and function of the brain. N-glycans have a distinct composition and undergo tight regulation in the brain, but the spatial distribution of these structures remains relatively unexplored. Here, we systematically employed carbohydrate binding lectins with differing specificities to various classes of N-glycans and appropriate controls to identify multiple regions of the mouse brain. Lectins binding high-mannose-type N-glycans, the most abundant class of brain N-glycans, showed diffuse staining with some punctate structures observed on high magnification. Lectins binding specific motifs of complex N-glycans, including fucose and bisecting GlcNAc, showed more partitioned labeling, including to the synapse-rich molecular layer of the cerebellum. Understanding the distribution of N-glycans across the brain will aid future studies of these critical protein modifications in development and disease of the brain.<\/jats:p>","DOI":"10.1101\/2023.05.30.542954","type":"posted-content","created":{"date-parts":[[2023,5,31]],"date-time":"2023-05-31T04:36:06Z","timestamp":1685507766000},"source":"Crossref","is-referenced-by-count":2,"title":["N-glycans show distinct spatial distribution in mouse brain"],"prefix":"10.64898","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2621-7374","authenticated-orcid":false,"given":"Maxence","family":"Noel","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8918-5034","authenticated-orcid":false,"given":"Richard D.","family":"Cummings","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5963-2836","authenticated-orcid":false,"given":"Robert G.","family":"Mealer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"54368","reference":[{"key":"2023060302200450000_2023.05.30.542954v1.1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev-neuro-071714-034019"},{"issue":"3","key":"2023060302200450000_2023.05.30.542954v1.2","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1172\/JCI131564","article-title":"Prion Protein Glycans Reduce Intracerebral Fibril Formation and Spongiosis in Prion Disease","volume":"130","year":"2020","journal-title":"J. Clin. Invest"},{"issue":"12","key":"2023060302200450000_2023.05.30.542954v1.3","doi-asserted-by":"crossref","first-page":"100433","DOI":"10.1016\/j.mcpro.2022.100433","article-title":"Glycoproteomics Landscape of Asymptomatic and Symptomatic Human Alzheimer\u2019s Disease Brain","volume":"21","year":"2022","journal-title":"Mol. Cell. Proteomics MCP"},{"key":"2023060302200450000_2023.05.30.542954v1.4","doi-asserted-by":"crossref","unstructured":"Mealer, R. G. ; Williams, S. E. ; Noel, M. ; Yang, B. ; D\u2019Souza, A. K. ; Nakata, T. ; Graham, D. B. ; Creasey, E. A. ; Cetinbas, M. ; Sadreyev, R. I. ; Scolnick, E. M. ; Woo, C. M. ; Smoller, J. W. ; Xavier, R. J. ; Cummings, R. D. The Schizophrenia-Associated Variant in SLC39A8 Alters Protein Glycosylation in the Mouse Brain. Mol. Psychiatry 2022. https:\/\/doi.org\/10.1038\/s41380-022-01490-1.","DOI":"10.1038\/s41380-022-01490-1"},{"issue":"3","key":"2023060302200450000_2023.05.30.542954v1.5","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1007\/s10719-022-10055-x","article-title":"The Dynamic Brain N-Glycome","volume":"39","year":"2022","journal-title":"Glycoconj. J"},{"key":"2023060302200450000_2023.05.30.542954v1.6","unstructured":"Cummings, R. D. ; Etzler, M. ; Hahn, M. G. ; Darvill, A. ; Godula, K. ; Woods, R. J. ; Mahal, L. K. Glycan-Recognizing Probes as Tools. In Essentials of Glycobiology; Varki, A. , Cummings, R. D. , Esko, J. D. , Stanley, P. , Hart, G. W. , Aebi, M. , Mohnen, D. , Kinoshita, T. , Packer, N. H. , Prestegard, J. H. , Schnaar, R. L. , Seeberger, P. H. , Eds.; Cold Spring Harbor Laboratory Press: Cold Spring Harbor (NY), 2022."},{"issue":"11","key":"2023060302200450000_2023.05.30.542954v1.7","doi-asserted-by":"crossref","first-page":"2993","DOI":"10.1021\/acschembio.1c00689","article-title":"A Useful Guide to Lectin Binding: Machine-Learning Directed Annotation of 57 Unique Lectin Specificities","volume":"17","year":"2022","journal-title":"ACS Chem. Biol"},{"key":"2023060302200450000_2023.05.30.542954v1.8","doi-asserted-by":"publisher","DOI":"10.1038\/srep43560"},{"issue":"1","key":"2023060302200450000_2023.05.30.542954v1.9","doi-asserted-by":"crossref","first-page":"100237","DOI":"10.1016\/j.xpro.2020.100237","article-title":"An Optimized Protocol for Combined Fluorescent Lectin\/Immunohistochemistry to Characterize Tissue-Specific Glycan Distribution in Human or Rodent Tissues","volume":"2","year":"2021","journal-title":"STAR Protoc"},{"issue":"19","key":"2023060302200450000_2023.05.30.542954v1.10","doi-asserted-by":"crossref","first-page":"12842","DOI":"10.1021\/acs.analchem.0c01206","article-title":"Region-Specific Characterization of N-Glycans in the Striatum and Substantia Nigra of an Adult Rodent Brain","volume":"92","year":"2020","journal-title":"Anal. Chem"},{"issue":"7","key":"2023060302200450000_2023.05.30.542954v1.11","doi-asserted-by":"crossref","first-page":"2400","DOI":"10.1016\/S0021-9258(17)30236-3","article-title":"Structural Determinants of Concanavalin A Specificity for Oligosaccharides","volume":"254","year":"1979","journal-title":"J. Biol. Chem"},{"issue":"7","key":"2023060302200450000_2023.05.30.542954v1.12","doi-asserted-by":"crossref","first-page":"2614","DOI":"10.1016\/S0021-9258(19)41645-1","article-title":"Interaction of Immunoglobulin Glycopeptides with Concanavalin A","volume":"250","year":"1975","journal-title":"J. Biol. Chem"},{"key":"2023060302200450000_2023.05.30.542954v1.13","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(89)79135-7"},{"issue":"11","key":"2023060302200450000_2023.05.30.542954v1.14","first-page":"1339","article-title":"The 2.0 A Structure of a Cross-Linked Complex between Snowdrop Lectin and a Branched Mannopentaose: Evidence for Two Unique Binding Modes","volume":"4","year":"1996","journal-title":"Struct. Lond. Engl. 1993"},{"issue":"8","key":"2023060302200450000_2023.05.30.542954v1.15","doi-asserted-by":"crossref","first-page":"4688","DOI":"10.1016\/S0021-9258(18)89125-6","article-title":"Fractionation of L-Fucose-Containing Oligosaccharides on Immobilized Aleuria Aurantia Lectin","volume":"260","year":"1985","journal-title":"J. Biol. Chem"},{"issue":"19","key":"2023060302200450000_2023.05.30.542954v1.16","doi-asserted-by":"crossref","first-page":"11230","DOI":"10.1016\/S0021-9258(18)33746-3","article-title":"Characterization of the Structural Determinants Required for the High Affinity Interaction of Asparagine-Linked Oligosaccharides with Immobilized Phaseolus Vulgaris Leukoagglutinating and Erythroagglutinating Lectins","volume":"257","year":"1982","journal-title":"J. Biol. Chem"},{"key":"2023060302200450000_2023.05.30.542954v1.17","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)75677-4"},{"key":"2023060302200450000_2023.05.30.542954v1.18","doi-asserted-by":"publisher","DOI":"10.1093\/glycob\/cwr080"},{"issue":"10","key":"2023060302200450000_2023.05.30.542954v1.19","doi-asserted-by":"crossref","first-page":"4576","DOI":"10.1016\/S0021-9258(18)68821-0","article-title":"The Immobilized Leukoag-glutinin from the Seeds of Maackia Amurensis Binds with High Affinity to Complex-Type Asn-Linked Oligosaccharides Containing Terminal Sialic Acid-Linked Alpha-2,3 to Penultimate Galactose Residues","volume":"263","year":"1988","journal-title":"J. Biol. Chem"},{"issue":"1","key":"2023060302200450000_2023.05.30.542954v1.20","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1038\/s41467-021-27781-9","article-title":"Mammalian Brain Glycoproteins Exhibit Diminished Glycan Complexity Compared to Other Tissues","volume":"13","year":"2022","journal-title":"Nat. Commun"},{"key":"2023060302200450000_2023.05.30.542954v1.21","doi-asserted-by":"crossref","unstructured":"Bradberry, M. M. ; Peters-Clarke, T. M. ; Shishkova, E. ; Chapman, E. R. ; Coon, J. J. Highly Fucosylated N-Glycans at the Synaptic Vesicle and Neuronal Plasma Membrane. bioRxiv July 19, 2022, p 2022.07.06.499060. https:\/\/doi.org\/10.1101\/2022.07.06.499060.","DOI":"10.1101\/2022.07.06.499060"},{"key":"2023060302200450000_2023.05.30.542954v1.22","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M116.764357"},{"key":"2023060302200450000_2023.05.30.542954v1.23","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2014207117"},{"key":"2023060302200450000_2023.05.30.542954v1.24","doi-asserted-by":"crossref","first-page":"711955","DOI":"10.3389\/fnana.2021.711955","article-title":"Mass Spectrometry Imaging for Glycome in the Brain","volume":"15","year":"2021","journal-title":"Front. Neuroanat"},{"key":"2023060302200450000_2023.05.30.542954v1.25","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.20609"}],"container-title":[],"original-title":[],"link":[{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1101\/2023.05.30.542954","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T04:42:56Z","timestamp":1768452176000},"score":1,"resource":{"primary":{"URL":"http:\/\/biorxiv.org\/lookup\/doi\/10.1101\/2023.05.30.542954"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,5,31]]},"references-count":25,"URL":"https:\/\/doi.org\/10.1101\/2023.05.30.542954","relation":{"is-preprint-of":[{"id-type":"doi","id":"10.1093\/glycob\/cwad077","asserted-by":"subject"}]},"subject":[],"published":{"date-parts":[[2023,5,31]]},"subtype":"preprint"}}