{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T07:39:18Z","timestamp":1778657958934,"version":"3.51.4"},"reference-count":58,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2017,8,28]],"date-time":"2017-08-28T00:00:00Z","timestamp":1503878400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["RO1NS090949"],"award-info":[{"award-number":["RO1NS090949"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[2018,3]]},"abstract":"<jats:sec><jats:label\/><jats:p>Agnoprotein (Agno) is an important regulatory protein of JC virus (JCV), BK virus (BKV) and simian virus 40 (SV40) and these viruses are unable to replicate efficiently in the absence of this protein. Recent 3D\u2010NMR structural data revealed that Agno contains two alpha\u2010helices (a minor and a major) while the rest of the protein adopts an unstructured conformation (Coric et al., 2017, J Cell Biochem). Previously, release of the JCV Agno from the Agno\u2010positive cells was reported. Here, we have further mapped the regions of Agno responsible for its release by a structure\u2010based systematic mutagenesis approach. Results revealed that amino acid residues (Lys22, Lys23, Phe31, Glu34, and Asp38) located either on or adjacent to the hydrophilic surface of the major alpha\u2010helix domain of Agno play critical roles in release. Additionally, Agno was shown to strongly interact with unidentified components of the cell surface when cells are treated with Agno, suggesting additional novel roles for Agno during the viral infection cycle.<\/jats:p><\/jats:sec>","DOI":"10.1002\/jcp.26106","type":"journal-article","created":{"date-parts":[[2017,7,19]],"date-time":"2017-07-19T12:36:45Z","timestamp":1500467805000},"page":"2343-2359","source":"Crossref","is-referenced-by-count":9,"title":["Structure\u2010based release analysis of the JC virus agnoprotein regions: A role for the hydrophilic surface of the major alpha helix domain in release"],"prefix":"10.1002","volume":"233","author":[{"given":"A. 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