{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,29]],"date-time":"2026-05-29T14:12:37Z","timestamp":1780063957320,"version":"3.54.0"},"reference-count":23,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2025,6,24]],"date-time":"2025-06-24T00:00:00Z","timestamp":1750723200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"},{"start":{"date-parts":[[2025,6,24]],"date-time":"2025-06-24T00:00:00Z","timestamp":1750723200000},"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":["Journal of Medical Virology"],"published-print":{"date-parts":[[2025,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Transmembrane protein 106B (TMEM106B) has been identified as a functional receptor facilitating ACE2\u2010independent SARS\u2010CoV\u20102 entry. However, its role in supporting a broad range of SARS\u2010CoV\u20102 variants, including the emerging Omicron BA.2.86 and JN.1 subvariants, remains to be determined. To address this question, we generated 293\u2010 and A549\u2010derived\n                    <jats:italic>TMEM106B<\/jats:italic>\n                    knockout cell lines and assessed their ability to support viral entry for various SARS\u2010CoV\u20102 variants (D614G, E484D, Omicron BA.1, BA.2, XBB.1.5, BA.2.86, and JN.1) using pseudoviral infection systems. We also examined the role of transmembrane protease serine 2 (TMPRSS2) and other type II transmembrane serine proteases (TTSP) in viral entry and syncytium formation. Our results showed that\n                    <jats:italic>TMEM106B<\/jats:italic>\n                    knockout significantly reduced viral entry across all tested variants. Additionally, overexpression of TMPRSS2, TMPRSS11F and TMPRSS13 in TMEM106B\u2010expressing cells enhanced viral entry and syncytium formation, including BA.2.86 and JN.1 variants. Importantly, we identified two single\u2010nucleotide polymorphisms (SNPs) that result in G2A and N151S variant, respectively, affects TMEM106B receptor function, indicating that selected genetic polymorphisms of\n                    <jats:italic>TMEM106B<\/jats:italic>\n                    gene may impact cell susceptibility to SARS\u2010CoV\u20102 infection. These findings highlight TMEM106B as a functional receptor for SARS\u2010CoV\u20102 across different variants, including the latest Omicron subvariants, and provide new insights for the therapeutic interventions targeting viral entry.\n                  <\/jats:p>","DOI":"10.1002\/jmv.70439","type":"journal-article","created":{"date-parts":[[2025,6,25]],"date-time":"2025-06-25T02:35:19Z","timestamp":1750818919000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["TMEM106B Supports Viral Entry and Syncytia Formation Mediated by the Spike Proteins From Omicron BA.2.86 and JN.1"],"prefix":"10.1002","volume":"97","author":[{"given":"Yuanyuan","family":"Wang","sequence":"first","affiliation":[{"name":"National Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, Beijing Ditan Hospital Capital Medical University Beijing China"},{"name":"Beijing Key Laboratory of Viral Infectious Disease, 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