{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,21]],"date-time":"2025-10-21T14:39:37Z","timestamp":1761057577378},"reference-count":26,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2003,2,15]],"date-time":"2003-02-15T00:00:00Z","timestamp":1045267200000},"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":[[2003,2,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Some poxviruses and their mammalian hosts encode homologous proteins that bind interleukin-18 (IL-18) with high affinity and inhibit IL-18-mediated immune responses. MC54L, the IL-18 binding protein of the human poxvirus that causes molluscum contagiosum, is unique in having a C-terminal tail of nearly 100 amino acids that is dispensable for IL-18 binding. When recombinant MC54L was expressed and purified via a C-terminal six-histidine tag, a shorter fragment was detected in addition to the full-length protein. This C-terminal fragment resulted from the cleavage of MC54L by cellular furin, as it was greatly diminished when furin was specifically inhibited or when a furin-deficient cell line was used for expression. Furthermore, the N- and C-terminal fragments of MC54L were generated by cleavage of the recombinant protein with furin in vitro. The furin cleavage site was mapped within a 32-amino-acid segment that is C terminal to the IL-18 binding domain. Full-length MC54L, but not the N-terminal IL-18 binding fragment, bound to cells and to purified heparin and other glycosaminoglycans that are commonly found on the cell surface and in the extracellular matrix. MC54L bound to heparin with a nanomolar\n            <jats:italic>\n              K\n              <jats:sub>d<\/jats:sub>\n            <\/jats:italic>\n            and could simultaneously bind to IL-18. Their different glycosaminoglycan and cell binding properties may allow the long and short forms of MC54L to inactivate IL-18 near the site of infection and at more distal locations, respectively.\n          <\/jats:p>","DOI":"10.1128\/jvi.77.4.2623-2630.2003","type":"journal-article","created":{"date-parts":[[2003,1,28]],"date-time":"2003-01-28T00:08:53Z","timestamp":1043712533000},"page":"2623-2630","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":37,"title":["Molluscum Contagiosum Virus Interleukin-18 (IL-18) Binding Protein Is Secreted as a Full-Length Form That Binds Cell Surface Glycosaminoglycans through the C-Terminal Tail and a Furin-Cleaved Form with Only the IL-18 Binding Domain"],"prefix":"10.1128","volume":"77","author":[{"given":"Yan","family":"Xiang","sequence":"first","affiliation":[{"name":"Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-0445"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bernard","family":"Moss","sequence":"additional","affiliation":[{"name":"Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-0445"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.164.6.3246"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.62.3.866-874.1988"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.2000.0689"},{"key":"e_1_3_2_5_2","first-page":"352","volume":"19","year":"1995","unstructured":"Carroll, M. W., and B. Moss. 1995. E. coli \u03b2-glucuronidase (GUS) as a marker for recombinant vaccinia viruses. BioTechniques 19 : 352-355.","journal-title":"BioTechniques"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(95)90352-6"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0091-6749(99)70518-X"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.82.10.3197"},{"key":"e_1_3_2_9_2","unstructured":"Esposito L. J. and F. Fenner. 2001. Poxviruses p. 2885-2921. In D. M. Knipe and P. M. Howley (ed.) Fields virology vol. 2. Lippincott Williams & Wilkins Philadelphia Pa."},{"key":"e_1_3_2_10_2","unstructured":"Fenner F. D. A. Henderson I. Arita Z. Jezek and I. D. Ladnyi. 1988. Smallpox and its eradication first ed. 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