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Open AccessArticle

Distinct MCM10 Proteasomal Degradation Profiles by Primate Lentiviruses Vpr Proteins

1
Viral Infectious Diseases Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
2
Laboratory of Viral Infectious Diseases, Department of Computational Biology and Medical Sciences, Graduate School of Frontier Science, The University of Tokyo, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
3
Photonics Control Technology Team, RIKEN Center for Advanced Photonics, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
4
Laboratory of Global Animal Resource Science, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
5
Nakamura Laboratory, Baton Zone program, Riken Cluster for Science, Technology and Innovation Hub, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
*
Author to whom correspondence should be addressed.
Viruses 2020, 12(1), 98; https://doi.org/10.3390/v12010098
Received: 11 November 2019 / Revised: 28 December 2019 / Accepted: 10 January 2020 / Published: 15 January 2020
(This article belongs to the Section Animal Viruses)
Viral protein R (Vpr) is an accessory protein found in various primate lentiviruses, including human immunodeficiency viruses type 1 and 2 (HIV-1 and HIV-2) as well as simian immunodeficiency viruses (SIVs). Vpr modulates many processes during viral lifecycle via interaction with several of cellular targets. Previous studies showed that HIV-1 Vpr strengthened degradation of Mini-chromosome Maintenance Protein10 (MCM10) by manipulating DCAF1-Cul4-E3 ligase in proteasome-dependent pathway. However, whether Vpr from other primate lentiviruses are also associated with MCM10 degradation and the ensuing impact remain unknown. Based on phylogenetic analyses, a panel of primate lentiviruses Vpr/x covering main virus lineages was prepared. Distinct MCM10 degradation profiles were mapped and HIV-1, SIVmus and SIVrcm Vprs induced MCM10 degradation in proteasome-dependent pathway. Colocalization and interaction between MCM10 with these Vprs were also observed. Moreover, MCM10 2-7 interaction region was identified as a determinant region susceptible to degradation. However, MCM10 degradation did not alleviate DNA damage response induced by these Vpr proteins. MCM10 degradation by HIV-1 Vpr proteins was correlated with G2/M arrest, while induction of apoptosis and oligomerization formation of Vpr failed to alter MCM10 proteolysis. The current study demonstrated a distinct interplay pattern between primate lentiviruses Vpr proteins and MCM10. View Full-Text
Keywords: primate lentiviruses; Vpr; MCM10; proteasomal degradation; DNA damage response; G2/M arrest primate lentiviruses; Vpr; MCM10; proteasomal degradation; DNA damage response; G2/M arrest
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Chang, H.; Siarot, L.; Matsuura, R.; Lo, C.-W.; Sato, H.; Otsuki, H.; Aida, Y. Distinct MCM10 Proteasomal Degradation Profiles by Primate Lentiviruses Vpr Proteins. Viruses 2020, 12, 98.

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