# HIV-1 and SUMOylation

Guillaume Beauclair, Ali Saïb, Alessia Zamborlini

► To cite this version:

Guillaume Beauclair, Ali Saïb, Alessia Zamborlini. HIV-1 and SUMOylation. Retrovirology, 2013, 10 (Suppl 1), pp.P106. 10.1186/1742-4690-10-S1-P106. inserm-00868804

HAL Id: inserm-00868804

https://inserm.hal.science/inserm-00868804v1

Submitted on 2 Oct 2013

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POSTER PRESENTATION

Open Access

HIV-1 and SUMOylation

Guillaume Beauclair<fnref n="1" />, Ali Saïb<fnref n="1" />,², Alessia Zamborlini<fnref n="1" />,²*

From Frontiers of Retrovirology: Complex retroviruses, retroelements and their hosts
Cambridge, UK. 16-18 September 2013

**Background**

The HIV virus hijacks cellular machineries to replicate. Post-translational modifications, like acetylation, phosphorylation or ubiquitination, are no exception. We are interested in studying the interplay between HIV and the SUMOylation pathway.

SUMOylation occurs via an enzymatic cascade requiring an E1 activating enzyme (SAE1/SAE2 heterodimer) and an E2 conjugating enzyme (Ubc9). This modification is reversible thanks to SUMO isopeptidases (SENPs). Despite Ubc9 alone being sufficient to transfer SUMO moieties to acceptor lysine residues *in vitro*, E3 SUMO ligases promote specificity and/or efficiency of SUMOylation *in vivo*. So far, several E3 SUMO ligases have been characterized, such as nuclear pore complex component Ran-binding protein 2 (RanBP2) and protein-inhibitor of activated STAT (PIAS) family proteins.

We have recently shown that HIV integrase, the viral enzyme that is responsible for viral genome integration into host cellular chromosome, is SUMOylated, and that virions harboring a SUMOylation-defective integrase are less infectious than WT viruses. Our data suggest that this modification is important for efficient viral replication.

**Materials and methods**

To detect protein SUMOylation, cells expressing Histagged SUMO protein together with the protein of interest (HIV integrase) were lysed in denaturing conditions followed by enrichment on NiNTA column. Bound proteins were eluted by boiling in Laemmli sample buffer supplemented with imidazole. Intracellular localization was studied by Duo LINK approach. Protein-protein interactions were analyzed by immunoprecipitation and GST pull-down assays.

**Results and conclusions**

To better characterize the involvement of SUMOylation during HIV replication, we are currently studying the role of E3 SUMO ligases and SENPs in the conjugation of SUMO to integrase. We established that HIV integrase interacts with PIAS family member proteins and we showed that integrase and PIAS colocalise. Moreover, we demonstrate that PIAS1 and PIAS4, but not other PIAS family members, increase whereas SENP1 decreases integrase SUMOylation. We also analyzed the effect of PIAS over-expression in virus-producing or target cells and do not find a significant variation of viral infectivity. Interestingly, during HIV infection we show a decrease of the expression levels of one of the members of PIAS family. Experiments are ongoing to elucidate the mechanisms underlying this interplay between HIV and the SUMOylation pathway.

**Authors' details**

¹CNRS/UP7 UMR7212, INSERM U944, Institut Universitaire d'Hématologie-Université Paris7 Diderot, Paris, 75010, France. ²Conservatoire des Arts et Métiers, Paris, 75003, France.

Published: 19 September 2013

doi:10.1186/1742-4690-10-S1-P106

Cite this article as: Beauclair *et al*. : HIV-1 and SUMOylation. *Retrovirology* 2013 10(Suppl 1):P106.

<footnote n="1">¹CNRS/UP7 UMR7212, INSERM U944, Institut Universitaire d'Hématologie-Université Paris7 Diderot, Paris, 75010, France
Full list of author information is available at the end of the article</footnote>