{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T15:57:00Z","timestamp":1761580620319},"reference-count":63,"publisher":"American Society for Microbiology","issue":"20","license":[{"start":{"date-parts":[[2008,10,15]],"date-time":"2008-10-15T00:00:00Z","timestamp":1224028800000},"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":[[2008,10,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Poxviruses are notorious for encoding multiple proteins that regulate cellular signaling pathways, including the ubiquitin-proteasome system. Bioinformatics indicated that ectromelia virus, the causative agent of lethal mousepox, encoded four proteins, EVM002, EVM005, EVM154, and EVM165, containing putative F-box domains. In contrast to cellular F-box proteins, the ectromelia virus proteins contain C-terminal F-box domains in conjunction with N-terminal ankyrin repeats, a combination that has not been previously reported for cellular proteins. These observations suggested that the ectromelia virus F-box proteins interact with SCF (\n            <jats:italic>S<\/jats:italic>\n            kp1,\n            <jats:italic>c<\/jats:italic>\n            ullin-1, and\n            <jats:italic>F<\/jats:italic>\n            -box) ubiquitin ligases. We focused our studies on EVM005, since this protein had only one ortholog in cowpox virus. Using mass spectrometry, we identified cullin-1 as a binding partner for EVM005, and this interaction was confirmed by overexpression of hemagglutinin (HA)-cullin-1. During infection, Flag-EVM005 and HA-cullin-1 colocalized to distinct cellular bodies. Significantly, EVM005 coprecipitated with endogenous Skp1, cullin-1, and Roc1 and associated with conjugated ubiquitin, suggesting that EVM005 interacted with the components of a functional ubiquitin ligase. Interaction of EVM005 with cullin-1 and Skp1 was abolished upon deletion of the F-box, indicating that the F-box played a crucial role in interaction with the SCF complex. Additionally, EVM002 and EVM154 interacted with Skp1 and conjugated ubiquitin, suggesting that ectromelia virus encodes multiple F-box-containing proteins that regulate the SCF complex. Our results indicate that ectromelia virus has evolved multiple proteins that interact with the SCF complex.\n          <\/jats:p>","DOI":"10.1128\/jvi.00953-08","type":"journal-article","created":{"date-parts":[[2008,8,7]],"date-time":"2008-08-07T00:46:33Z","timestamp":1218069993000},"page":"9917-9927","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":38,"title":["Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex"],"prefix":"10.1128","volume":"82","author":[{"given":"Nick","family":"van Buuren","sequence":"first","affiliation":[{"name":"Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Brianne","family":"Couturier","sequence":"additional","affiliation":[{"name":"Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yue","family":"Xiong","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michele","family":"Barry","sequence":"additional","affiliation":[{"name":"Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.80.10.4978-4991.2006"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.74.8.3815-3831.2000"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1042\/bse0410015"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80098-7"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.00734-07"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1007\/s11262-005-0035-7"},{"key":"e_1_3_2_8_2","first-page":"pe21","volume":"2006","year":"2006","unstructured":"Barry, M., and K. 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