Vpr and its cellular interaction partners: R we there yet?

H Fabryova, K Strebel - Cells, 2019 - mdpi.com
Vpr is a lentiviral accessory protein that is expressed late during the infection cycle and is
packaged in significant quantities into virus particles through a specific interaction with the …

HIV-1 Vpr degrades the HLTF DNA translocase in T cells and macrophages

H Lahouassa, ML Blondot… - Proceedings of the …, 2016 - National Acad Sciences
Viruses often interfere with the DNA damage response to better replicate in their hosts. The
human immunodeficiency virus 1 (HIV-1) viral protein R (Vpr) protein has been reported to …

HIV-1 and HIV-2 exhibit divergent interactions with HLTF and UNG2 DNA repair proteins

K Hrecka, C Hao, MC Shun, S Kaur… - Proceedings of the …, 2016 - National Acad Sciences
HIV replication in nondividing host cells occurs in the presence of high concentrations of
noncanonical dUTP, apolipoprotein B mRNA-editing, enzyme-catalytic, polypeptide-like 3 …

Neddylation inhibitor MLN4924 has anti‐HBV activity via modulating the ERK‐HNF1α‐C/EBPα‐HNF4α axis

M Xie, H Guo, G Lou, J Yao, Y Liu, Y Sun… - Journal of Cellular …, 2021 - Wiley Online Library
Hepatitis B virus (HBV) infection is a major public health problem. The high levels of HBV
DNA and HBsAg are positively associated with the development of secondary liver …

Ubiquitination and SUMOylation in HIV infection: Friends and foes

M Colomer-Lluch, S Castro-Gonzalez… - Current issues in …, 2020 - mdpi.com
As intracellular parasites, viruses hijack the cellular machinery to facilitate their replication
and spread. This includes favouring the expression of their viral genes over host genes …

SLX4-SLX1 Protein-independent Down-regulation of MUS81-EME1 Protein by HIV-1 Viral Protein R (Vpr)*♦

X Zhou, M DeLucia, J Ahn - Journal of Biological Chemistry, 2016 - ASBMB
Evolutionarily conserved structure-selective endonuclease MUS81 forms a complex with
EME1 and further associates with another endonuclease SLX4-SLX1 to form a four-subunit …

Activation of the DNA damage response is a conserved function of HIV-1 and HIV-2 Vpr that is independent of SLX4 recruitment

OI Fregoso, M Emerman - MBio, 2016 - Am Soc Microbiol
There has been extraordinary progress in understanding the roles of lentiviral accessory
proteins in antagonizing host antiviral defense proteins. However, the precise primary …

Virion encapsidated HIV-1 Vpr induces NFAT to prime non-activated T cells for productive infection

K Höhne, R Businger, A Van Nuffel… - Open …, 2016 - royalsocietypublishing.org
The majority of T cells encountered by HIV-1 are non-activated and do not readily allow
productive infection. HIV-1 Vpr is highly abundant in progeny virions, and induces signalling …

HIV-1 Vpr protein directly loads helicase-like transcription factor (HLTF) onto the CRL4-DCAF1 E3 ubiquitin ligase

X Zhou, M DeLucia, C Hao, K Hrecka, C Monnie… - Journal of Biological …, 2017 - ASBMB
The viral protein R (Vpr) is an accessory virulence factor of HIV-1 that facilitates infection in
immune cells. Cellular functions of Vpr are tied to its interaction with DCAF1, a substrate …

HIV-1 Vpr causes separate cell cycle arrests in G2 and M that activate alternative DNA damage pathways

R Hall, LM Ahern, MW Yap, MHC Tsai, VC Boucherit… - bioRxiv, 2024 - biorxiv.org
Vpr is a conserved primate lentiviral accessory protein that induces cell cycle arrest in G2.
The precise mechanism of this arrest and its benefit to viral replication is unknown. Here, we …