The Baculoviridae family of viruses encode a viral Ubiquitin (vUb) gene. Though the vUb is homologous to the host eukaryotic Ubiquitin (Ub), its preservation in the viral genome indicates unique functions that are not compensated by the host Ub. We report the structural, biophysical, and biochemical properties of the vUb from Autographa californica multiple nucleo-polyhedrosis virus (AcMNPV). The packing of central helix α1 to the beta-sheet β1–β5 is different between vUb and Ub. Consequently, its stability is lower compared with Ub. However, the surface properties, ubiquitination activity, and the interaction with Ubiquitin-binding domains are similar between vUb and Ub. Interestingly, vUb forms atypical polyubiquitin chain linked by lysine at the 54th position (K54), and the deubiquitinating enzymes are ineffective against the K54-linked polyubiquitin chains. We propose that the modification of host/viral proteins with the K54-linked chains is an effective way selected by the virus to protect the vUb signal from host DeUbiquitinases.
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Cover Image
Cover Image
The Autographa californica Multiple Nucleo-Polyhedrosis virus encodes for a variant of Ubiquitin molecule that can create atypical linkages mediated by Lysine 54 (shown in red). We show that the Ubiquitin signalling via the atypical chains is protected from the host Deubiquitinase enzymes, which possibly allows the virus to circumvent antiviral responses. For more information, see the article by Negi and colleagues in this issue (pp. 2193–2219). The image was provided by Ranabir Das.
A novel polyubiquitin chain linkage formed by viral Ubiquitin is resistant to host deubiquitinating enzymes
Hitendra Negi, Pothula Purushotham Reddy, Vineeth Vengayil, Chhaya Patole, Sunil Laxman, Ranabir Das; A novel polyubiquitin chain linkage formed by viral Ubiquitin is resistant to host deubiquitinating enzymes. Biochem J 26 June 2020; 477 (12): 2193–2219. doi: https://doi.org/10.1042/BCJ20200289
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