{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,8]],"date-time":"2026-07-08T11:40:36Z","timestamp":1783510836456,"version":"3.55.0"},"reference-count":60,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2009,4,1]],"date-time":"2009-04-01T00:00:00Z","timestamp":1238544000000},"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":[[2009,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>Poxviruses express proteins that limit host immune responses to infection. For example, the molluscum contagiosum virus MC160 protein inhibits tumor necrosis factor alpha (TNF-\u03b1)-induced NF-\u03baB activation. This event correlates with MC160-induced IKK1 protein degradation, suggesting a mechanism for the above-mentioned phenotype. IKK1 is stabilized when it associates with the cellular heat shock protein 90 (Hsp90). Here, Hsp90 overexpression restored IKK1 levels in MC160-expressing cells, suggesting that MC160 competitively interacted with Hsp90. In support of this, further investigation showed that a mutant MC160 protein comprising only the C-terminal region (C protein) immunoprecipitated with Hsp90. In contrast, Hsp90 IP with a mutant MC160 protein consisting of only the N-terminal tandem death effector domains (DEDs) (N protein) was dramatically decreased. Since cells expressing either the N or C mutant MC160 protein remained similarly resistant to TNF-\u03b1-induced NF-\u03baB activation, the N mutant protein probably utilized a different mechanism for inhibiting NF-\u03baB. One likely mechanism for the N protein lies in its association with the DED-containing procaspase-8 protein, a cellular apoptosis precursor protein that regulates NF-\u03baB activation. Here, IPs revealed that this association relied on the presence of the DED-containing N terminus of the MC160 protein but not the C-terminal portion. These interactions appear to have relevance with NF-\u03baB activation, since the expression of the viral DEDs strongly inhibited procaspase-8-mediated NF-\u03baB activation, an event not substantially altered by the C protein. Thus, the MC160 protein utilizes at least two distinct mechanisms for impeding NF-\u03baB activation, association with Hsp90 to result in IKK1 protein degradation or interaction with procaspase-8.<\/jats:p>","DOI":"10.1128\/jvi.02009-08","type":"journal-article","created":{"date-parts":[[2009,1,22]],"date-time":"2009-01-22T02:09:45Z","timestamp":1232590185000},"page":"3162-3174","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":31,"title":["Poxvirus MC160 Protein Utilizes Multiple Mechanisms To Inhibit NF-\u03baB Activation Mediated via Components of the Tumor Necrosis Factor Receptor 1 Signal Transduction Pathway"],"prefix":"10.1128","volume":"83","author":[{"given":"Daniel Brian","family":"Nichols","sequence":"first","affiliation":[{"name":"Department of Microbiology, College of Medicine, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joanna L.","family":"Shisler","sequence":"additional","affiliation":[{"name":"Department of Microbiology, College of Medicine, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature01648"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1159\/000117709"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.1.376"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.it.2004.03.008"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.160027697"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.onc.1207705"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.onc.1203812"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.onc.1202976"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1097-2765(02)00450-1"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1071924"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.0040022"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.9.13.1586"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M102941200"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0002-9394(02)01499-X"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.95.11.6403"},{"key":"e_1_3_2_17_2","first-page":"2947","volume":"2","year":"2007","unstructured":"Damon, I. 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