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the ND10 bodies become viral replication compartments, and ICP0, a viral E3 ligase, degrades both PML and SP100. The amounts of PML and SP100 and the number of ND10 structures increase in cells exposed to IFN-beta.
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that Sp100 represses viral transcription and replication in differentiated cells
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Data suggest that nuclear antigen Sp100C is a multifaceted histone H3 methylation and phosphorylation sensor.
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These results suggest that high-risk human papillomavirus 31 target interferon kappa to prevent Sp100 expression and identify Sp100 as an interferon-stimulated gene with anti-human papillomavirus activity.
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PML, hDaxx and Sp100 primarily act as cellular restriction factors during lytic human cytomegalovirus replication and during the dynamic process of reactivation but do not serve as key determinants for the establishment of latency.
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Sp100 repressed viral transcription and replication only during the initial stages of viral establishment, suggesting that Sp100 acts as a repressor of incoming human papillomavirus type 18 DNA.
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Sp100 depletion promotes Adenovirus progeny production and early viral protein synthesis.
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Two regions within the N-terminal of the herpes simplex virus 1 ICP0 facilitate the degradation and dissociation of host PML and dissociation of Sp100 from ND10.
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Sp100 is recruited to activated arrays in cells expressing the herpes simplex virus type 1 E3 ubiquitin ligase, ICP0, which degrades all Sp100 isoforms except unsumoylated Sp100A.
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The results suggest that hantavirus infection interferes with DAXX-mediated apoptosis, and expression of interferon-activated Sp100 and ISG-20 proteins may indicate intracellular intrinsic antiviral attempts.
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SP100 and Adeno-associated virus 2 Rep78 are both located in the nucleolus, which provides the spatial possibility for their interaction.
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Authors conclude that several ND10 components, including Daxx, the promyelocytic leukemia (PML) protein, and Sp100 cooperate in an additive manner to regulate herpes simplex virus type 1 and human cytomegalovirus infection.
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Herpesvirus saimiri tegument protein specifically degraded the cellular ND10 component Sp100.
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These findings expand our knowledge of both Sp100 and Cdc20 as well as their role in ubiquitination.
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These findings indicate that thehuman herpesvirus 5 IE1-dependent loss of human Sp100 proteins during virus infection may represent an important requirement for efficient viral growth.
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Taken together, these data provide evidence that Sp100 is the first ND10-related factor identified that not only possesses the potential to restrict the initial stage of infection but also inhibits cytomegalovirus replication during the late phase.
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Sp100 counteract human cytomegalovirus infection via the repression of viral immediate-early gene expression.
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SP100 expression reduces malignancy of brain tumors
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Endogenous Sp100 may interact with PhiC31 integrase and inhibit the efficiency of PhiC31 integrase-mediated recombination.
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Sp100 has a role in the initiation and progression of tumorgenesis
