{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T00:40:05Z","timestamp":1792716005681,"version":"4.5.0"},"reference-count":83,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T00:00:00Z","timestamp":1792627200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"},{"start":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T00:00:00Z","timestamp":1792627200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["NS045585"],"award-info":[{"award-number":["NS045585"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["NS129502"],"award-info":[{"award-number":["NS129502"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["NS115876"],"award-info":[{"award-number":["NS115876"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Brain Pathology"],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Microglia constitute a major innate defense mechanism against prion infection; however, the molecular pathways regulating microglial responses during disease progression remain incompletely understood. Galectin\u20103 (Gal3), a \u03b2\u2010galactoside\u2010binding lectin associated with reactive microglia in multiple neurodegenerative disorders, has been implicated in phagocytosis, inflammatory signaling, and lysosomal homeostasis. Here, we investigated the role of Gal3 in prion disease pathogenesis using prion\u2010infected mice. Gal3 expression was undetectable in healthy brain but became upregulated beginning at late preclinical stages, increasing with disease progression. Gal3 localized predominantly to a subpopulation of reactive IBA1\u2010positive microglia, particularly within the thalamus, and inversely correlated with expression of the homeostatic microglial markers P2Y12 and TMEM119, consistent with acquisition of a reactive phenotype. Microglia engaged in neuronal envelopment displayed elevated Gal3 expression during terminal disease. Constitutive deletion of Gal3 significantly accelerated clinical disease progression without altering total PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    accumulation, reactive gliosis, neuronal envelopment, or overall microglial and astrocytic activation. However, Gal3 deficiency markedly reduced microglial uptake of PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    , resulting in a lower intracellular\u2010to\u2010extracellular PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    ratio, supporting a role for Gal3 in phagocytic sequestration of prions. In contrast, Gal3 deficiency did not impair lysosomal activity, lysosomal membrane integrity, or expression of genes involved in lysosomal repair pathways. Likewise, selective inhibition of autophagy in myeloid cells exerted only minor effects on disease progression. Collectively, these findings identify Gal3 as a sensitive marker of reactive microglia that contributes to microglial uptake of PrP\n                    <jats:sup>Sc<\/jats:sup>\n                    and exerts a protective role during prion disease progression.\n                  <\/jats:p>","DOI":"10.1111\/bpa.70161","type":"journal-article","created":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T00:15:48Z","timestamp":1792714548000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Protective role of Galectin\u20103 in prion disease through regulation of microglial\n                    <scp>\n                      PrP\n                      <sup>Sc<\/sup>\n                    <\/scp>\n                    uptake"],"prefix":"10.1111","author":[{"given":"Natallia","family":"Makarava","sequence":"first","affiliation":[{"name":"Department of Neurobiology University of Maryland School of Medicine  Baltimore Maryland USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tarek","family":"Safadi","sequence":"additional","affiliation":[{"name":"Department of Neurobiology University of Maryland School of Medicine  Baltimore Maryland USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Narayan P.","family":"Pandit","sequence":"additional","affiliation":[{"name":"Department of Neurobiology University of Maryland School of Medicine  Baltimore Maryland USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olga","family":"Mychko","sequence":"additional","affiliation":[{"name":"Department of Neurobiology University of Maryland School of Medicine  Baltimore Maryland USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5056-1506","authenticated-orcid":false,"given":"Olga","family":"Bocharova","sequence":"additional","affiliation":[{"name":"Department of Neurobiology University of Maryland School of Medicine  Baltimore Maryland USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexey","family":"Shevelkin","sequence":"additional","affiliation":[{"name":"Department of Neurobiology University of Maryland School of Medicine  Baltimore Maryland USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kara","family":"Molesworth","sequence":"additional","affiliation":[{"name":"Department of Neurobiology University of Maryland School of Medicine  Baltimore Maryland USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7537-9014","authenticated-orcid":false,"given":"Marta M.","family":"Lipinski","sequence":"additional","affiliation":[{"name":"Department of Neurobiology University of Maryland School of Medicine  Baltimore Maryland USA"},{"name":"Department of Anesthesiology and Center for Shock, Trauma and Anesthesiology Research (STAR) University of Maryland School of Medicine  Baltimore Maryland USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2821-0942","authenticated-orcid":false,"given":"Ilia V.","family":"Baskakov","sequence":"additional","affiliation":[{"name":"Department of Neurobiology University of Maryland School of Medicine  Baltimore Maryland USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,10,22]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"crossref","first-page":"13363","DOI":"10.1073\/pnas.95.23.13363","article-title":"Prions","volume":"95","author":"Prusiner SB","year":"1998","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"4542","key":"e_1_2_9_3_1","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1126\/science.6801762","article-title":"Novel proteinaceous infectious particles cause scrapie","volume":"216","author":"Prusiner SB","year":"1982","journal-title":"Science"},{"key":"e_1_2_9_4_1","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1146\/annurev.biochem.67.1.793","article-title":"Pathologic conformations of prion proteins","volume":"67","author":"Cohen FE","year":"1998","journal-title":"Annu Rev Biochem"},{"issue":"5","key":"e_1_2_9_5_1","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005623","article-title":"A neuronal culture system to detect prion synaptotoxicity","volume":"12","author":"Fang C","year":"2016","journal-title":"PLoS Pathog"},{"issue":"9","key":"e_1_2_9_6_1","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1007283","article-title":"Prions activate a p38 MAPK synaptotoxic signaling pathway","volume":"14","author":"Fang C","year":"2018","journal-title":"PLoS Pathog"},{"key":"e_1_2_9_7_1","doi-asserted-by":"crossref","first-page":"1514","DOI":"10.1126\/science.1094273","article-title":"Cross\u2010linking cellular prion protein triggers neuronal apoptosis in vivo","volume":"303","author":"Solforosi L","year":"2004","journal-title":"Science"},{"key":"e_1_2_9_8_1","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1038\/379339a0","article-title":"Normal host prion protein necessary for scrapie\u2010induced neurotoxicity","volume":"379","author":"Brandner S","year":"1996","journal-title":"Nature"},{"key":"e_1_2_9_9_1","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1126\/science.1090187","article-title":"Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis","volume":"302","author":"Mallucci G","year":"2003","journal-title":"Science"},{"issue":"2","key":"e_1_2_9_10_1","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.tins.2011.10.002","article-title":"Prion protein at the crossroads of physiology and disease","volume":"35","author":"Biasini E","year":"2012","journal-title":"Trends Neurosci"},{"issue":"14","key":"e_1_2_9_11_1","doi-asserted-by":"crossref","first-page":"1974","DOI":"10.1038\/emboj.2008.122","article-title":"Stress\u2010protective signalling of prion protein is corrupted by scrapie prions","volume":"27","author":"Rambold AS","year":"2008","journal-title":"EMBO J"},{"issue":"1","key":"e_1_2_9_12_1","doi-asserted-by":"crossref","DOI":"10.3390\/v11010065","article-title":"Neuroinflammation, microglia, and cell\u2010association during prion disease","volume":"11","author":"Carroll JA","year":"2019","journal-title":"Viruses"},{"issue":"9","key":"e_1_2_9_13_1","doi-asserted-by":"crossref","first-page":"3230","DOI":"10.1172\/JCI90605","article-title":"Microglia in prion diseases","volume":"127","author":"Aguzzi A","year":"2017","journal-title":"J Clin Invest"},{"issue":"19","key":"e_1_2_9_14_1","doi-asserted-by":"crossref","DOI":"10.3390\/ijms21197299","article-title":"The effects of immune system modulation on prion disease susceptibility and pathogenesis","volume":"21","author":"Mabbott NA","year":"2020","journal-title":"Int J Mol Sci"},{"issue":"11","key":"e_1_2_9_15_1","doi-asserted-by":"crossref","first-page":"2169","DOI":"10.1002\/glia.24244","article-title":"Microglia deficiency accelerates prion disease but does not enhance prion accumulation in the brain","volume":"70","author":"Bradford BM","year":"2022","journal-title":"Glia"},{"issue":"15","key":"e_1_2_9_16_1","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00549-18","article-title":"Microglia are critical in host defense against prion disease","volume":"92","author":"Carroll JA","year":"2018","journal-title":"J Virol"},{"issue":"1","key":"e_1_2_9_17_1","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1186\/s13041-020-00610-8","article-title":"RNA\u2010seq and network analysis reveal unique glial gene expression signatures during prion infection","volume":"13","author":"Carroll JA","year":"2020","journal-title":"Mol 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cells","volume":"16","author":"Patnaik SK","year":"2005","journal-title":"Glycobiology"},{"issue":"52","key":"e_1_2_9_27_1","doi-asserted-by":"crossref","first-page":"20249","DOI":"10.1074\/jbc.RA118.004636","article-title":"Galectin binding to cells and glycoproteins with genetically modified glycosylation reveals galectin\u2010glycan specificities in a natural context","volume":"293","author":"Nielsen MI","year":"2018","journal-title":"J Biol Chem"},{"issue":"1","key":"e_1_2_9_28_1","doi-asserted-by":"crossref","first-page":"3473","DOI":"10.1038\/s41467-019-11441-0","article-title":"Galectin\u20103 is required for the microglia\u2010mediated brain inflammation in a model of Huntington's disease","volume":"10","author":"Siew JJ","year":"2019","journal-title":"Nat Commun"},{"issue":"9","key":"e_1_2_9_29_1","doi-asserted-by":"crossref","first-page":"1626","DOI":"10.1016\/j.celrep.2015.02.012","article-title":"Microglia\u2010secreted galectin\u20103 acts as a toll\u2010like receptor 4 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disease","volume":"138","author":"Boza\u2010Serrano A","year":"2019","journal-title":"Acta Neuropathol"},{"issue":"1","key":"e_1_2_9_33_1","article-title":"The role of galectin\u20103 in \u03b1\u2010synuclein\u2010induced microglial activation","volume":"2","author":"Boza\u2010Serrano A","year":"2014","journal-title":"Acta Neuropathol Commun"},{"issue":"2","key":"e_1_2_9_34_1","doi-asserted-by":"crossref","DOI":"10.1172\/JCI165523","article-title":"Galectin\u20103 aggravates microglial activation and tau transmission in tauopathy","volume":"134","author":"Siew JJ","year":"2024","journal-title":"J Clin Invest"},{"key":"e_1_2_9_35_1","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-026-73003-5","article-title":"Gpnmb defines a phagocytic state of microglia linked to cell death in prion disease mouse model","volume":"17","author":"Caredio D","year":"2026","journal-title":"Nat 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