{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,5]],"date-time":"2026-09-05T09:06:32Z","timestamp":1788599192520,"version":"build-2803163510"},"reference-count":46,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2025,4,21]],"date-time":"2025-04-21T00:00:00Z","timestamp":1745193600000},"content-version":"vor","delay-in-days":20,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Biology of the Cell"],"published-print":{"date-parts":[[2025,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>SARS\u2010CoV\u20102 has led to significant global health and economic challenges and caused the COVID\u201019 pandemic. The ability of the virus to replicate adeptly within host cells is critical for its pathogenicity. The structural nucleocapsid (N) protein of SARS\u2010CoV\u20102 packages newly synthesized viral RNA with the association of various host proteins that may contribute to different functions in maintaining a productive viral life cycle. In this study, we report the identification and characterization of host proteins SFPQ and hnRNP U interacting with SARS\u2010CoV\u20102 N protein in both N\u2010transfected cells and virus\u2010infected cells, forming a hetero\u2010trimeric protein complex. Using carefully designed peptides that span the length of N protein and competitive inhibition, we identified the interacting domains at N protein that interact with SFPQ and hnRNP U. Our results constitute the first report that the characterized N protein and host SFPQ and hnRNP U form a hetero\u2010trimeric protein complex in both N transfected cells and virus\u2010infected cells. Utilizing competitive peptides, we were able to disrupt the hetero\u2010trimeric protein complex in virus\u2010infected cells, leading to reduction in viral replication. These results clearly demonstrate that N\u2010SFPQ\u2010hnRNP U hetero\u2010trimeric protein complex formation is found in SARS\u2010CoV\u20102 infected cells that regulate viral replication. Our findings suggest that the protein\u2013protein interaction (PPI) between N\u2010SFPQ\u2010hnRNP U hetero\u2010trimeric protein complexes could be a novel drug target for developing therapeutics against COVID\u201019.<\/jats:p>","DOI":"10.1111\/boc.70008","type":"journal-article","created":{"date-parts":[[2025,4,22]],"date-time":"2025-04-22T04:09:55Z","timestamp":1745294995000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Identification and Characterization of a Novel Protein\u2013Protein Interaction Among SARS\u2010CoV\u20102 Nucleocapsid, Host SFPQ, and hnRNP U and Its Potential Role in Virus Replication"],"prefix":"10.1111","volume":"117","author":[{"given":"Ashish","family":"Agrahari","sequence":"first","affiliation":[{"name":"Division of Virus Research and Therapeutics Central Drug Research Institute Council of Scientific &amp; Industrial Research  Uttar Pradesh India"},{"name":"Academy of Scientific &amp; Innovative Research (AcSIR) Ghaziabad Uttar Pradesh India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Km.","family":"Archana","sequence":"additional","affiliation":[{"name":"Division of Virus Research and Therapeutics Central Drug Research Institute Council of Scientific &amp; Industrial Research  Uttar Pradesh India"},{"name":"Academy of Scientific &amp; Innovative Research (AcSIR) Ghaziabad Uttar Pradesh India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nittu","family":"Singh","sequence":"additional","affiliation":[{"name":"CSIR\u2010Institute of Microbial Technology Chandigarh India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akshay","family":"Joshi","sequence":"additional","affiliation":[{"name":"CSIR\u2010Institute of Microbial Technology Chandigarh India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Budai S. 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