{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,29]],"date-time":"2026-03-29T12:21:52Z","timestamp":1774786912962,"version":"3.50.1"},"reference-count":31,"publisher":"American Society for Microbiology","issue":"21","license":[{"start":{"date-parts":[[2006,11,1]],"date-time":"2006-11-01T00:00:00Z","timestamp":1162339200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2006,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>The orthopoxviruses ectromelia virus (ECTV) and vaccinia virus (VACV) express secreted gamma interferon binding proteins (IFN-\u03b3BPs) with homology to the ligand binding domains of the host's IFN-\u03b3 receptor (IFN-\u03b3R1). Homology between these proteins is limited to the extracellular portions of the IFN-\u03b3R1 and the first \u223c200 amino acids of the IFN-\u03b3BPs. The remaining 60 amino acids at the C termini of the IFN-\u03b3BPs contain a single cysteine residue shown to be important in covalent dimerization of the secreted proteins. The function of the remaining C-terminal domain (CTD) has remained elusive, yet this region is conserved within all orthopoxvirus IFN-\u03b3BPs. Using a series of C-terminal deletion constructs, we have determined that the CTD is essential for IFN-\u03b3 binding despite having no predicted homology to the IFN-\u03b3R1. Truncation of the ECTV IFN-\u03b3BP by more than two amino acid residues results in a complete loss of binding activity for both murine IFN-\u03b3 and human IFN-\u03b3 (hIFN-\u03b3), as measured by surface plasmon resonance (SPR) and bioassay. Equivalent truncation of the VACV IFN-\u03b3BP resulted in comparable loss of hIFN-\u03b3 binding activity by SPR. Full-length IFN-\u03b3BPs were observed to form higher-ordered structures larger than the previously reported dimers. Mutants that were unable to bind IFN-\u03b3 with high affinity in SPR experiments failed to assemble into these higher-ordered structures and migrated as dimers. We conclude that the unique CTD of orthopoxvirus IFN-\u03b3BPs is important for the assembly of covalent homodimers as well as the assembly of higher-ordered structures essential for IFN-\u03b3 binding.<\/jats:p>","DOI":"10.1128\/jvi.01015-06","type":"journal-article","created":{"date-parts":[[2006,10,15]],"date-time":"2006-10-15T06:42:36Z","timestamp":1160894556000},"page":"10675-10682","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":12,"title":["The Unique C Termini of Orthopoxvirus Gamma Interferon Binding Proteins Are Essential for Ligand Binding"],"prefix":"10.1128","volume":"80","author":[{"given":"Anthony A.","family":"Nuara","sequence":"first","affiliation":[{"name":"Department of Molecular Microbiology and Immunology, Saint Louis University Health Sciences Center, St. Louis, Missouri 63104"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hongdong","family":"Bai","sequence":"additional","affiliation":[{"name":"Department of Cell Biology, Division of Vascular Biology, Scripps Research Institute, La Jolla, California 92037"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nanhai","family":"Chen","sequence":"additional","affiliation":[{"name":"Genelux Corporation, San Diego, California 92109"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R. 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