Nathalie J. Arhel

Université de Montpellier

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Sébastien Nisole

Institut de Recherche en Infectiologie de Montpellier

Pierre Charneau

Theravectys (France)

Juliette Fernandez

Centre National de la Recherche Scientifique

Ghizlane Maarifi

Université de Montpellier

Frank Kirchhoff

University Medical Center

Débora M. Portilho

Sorbonne Université

Sandie Munier

Centre National de la Recherche Scientifique

Francesca Di Nunzio

Institut Pasteur

Spencer Shorte

Institut Pasteur

Jacques Dutrieux

Inserm

Cooperative Institutions

Centre National de la Recherche Scientifique

125

Inserm

Université Paris Cité

Institut Pasteur

Université de Montpellier

Institut de Recherche en Infectiologie de Montpellier

Department of Virology

Université Paris-Saclay

Sorbonne Paris Cité

Commissariat à l'Énergie Atomique et aux Énergies Alternatives

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Alarmin S100A9 restricts retroviral infection by limiting reverse transcription in human dendritic cells

The EMBO Journal (2021)

Ghizlane Maarifi Justine Lagisquet Quentin Hertel Boris Bonaventure Célia Chamontin

10.15252/embj.2020106540

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Citations (15)

HIV-1 capsid interacts with cytoskeletal-associated proteins for intracytoplasmic routing to the nucleus

Retrovirology (2013)

Juliette Fernandez Kathleen Gärtner Andreas Becker Anne Danckaert Sandie Munier

Background During infection, the Human Immunodeficiency Virus type 1 (HIV-1) uses the host cytoskeleton to traffic across the cytoplasm to the nucleus where its genome integrates into the host DNA. We have previously shown that HIV retrograde transport (i.e. towards the nucleus) results from the successive transfers from fast microtubule-directed movement to slower actinmediated movement closer to the nuclear compartment, resulting in docking at the nuclear pore [1]. However, neither the cellular cytoplasmic component(s) nor the viral protein(s) that interact to mediate transport have yet been identified. Recent data show that HIV-1 uncoating does not occur immediately after cell entry but near the nuclear membrane, suggesting that the viral structure interacting with the cytoskeleton during early retrograde trafficking might be the capsid.

Nuclear pore

Transport protein

10.1186/1742-4690-10-s1-p34

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Superresolution imaging of HIV in infected cells with FlAsH-PALM

Proceedings of the National Academy of Sciences (2012)

Mickaël Lelek Francesca Di Nunzio Ricardo Henriques Pierre Charneau Nathalie J. Arhel

Imaging protein assemblies at molecular resolution without affecting biological function is a long-standing goal. The diffraction-limited resolution of conventional light microscopy (∼200-300 nm) has been overcome by recent superresolution (SR) methods including techniques based on accurate localization of molecules exhibiting stochastic fluorescence; however, SR methods still suffer important restrictions inherent to the protein labeling strategies. Antibody labels are encumbered by variable specificity, limited commercial availability and affinity, and are mostly restricted to fixed cells. Fluorescent protein fusions, though compatible with live cell imaging, substantially increase protein size and can interfere with their biological activity. We demonstrate SR imaging of proteins tagged with small tetracysteine motifs and the fluorescein arsenical helix binder (FlAsH-PALM). We applied FlAsH-PALM to image the integrase enzyme (IN) of HIV in fixed and living cells under experimental conditions that fully preserved HIV infectivity. The obtained resolution (∼30 nm) allowed us to characterize the distribution of IN within virions and intracellular complexes and to distinguish different HIV structural populations based on their morphology. We could thus discriminate ∼100 nm long mature conical cores from immature Gag shells and observe that in infected cells cytoplasmic (but not nuclear) IN complexes display a morphology similar to the conical capsid. Together with the presence of capsid proteins, our data suggest that cytoplasmic IN is largely present in intact capsids and that these can be found deep within the cytoplasm. FlAsH-PALM opens the door to in vivo SR studies of microbial complexes within host cells and may help achieve truly molecular resolution.

Fluorescence-lifetime imaging microscopy

10.1073/pnas.1013267109

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Citations (149)

Role of Nef in primate lentiviral immunopathogenesis

Cellular and Molecular Life Sciences (2008)

Frank Kirchhoff Michael Schindler Anke Specht Nathalie J. Arhel Jan Münch

Simian immunodeficiency virus

Rhesus macaque

Simian

10.1007/s00018-008-8094-2

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Citations (116)

Nuclear Import Defect of Human Immunodeficiency Virus Type 1 DNA Flap Mutants Is Not Dependent on the Viral Strain or Target Cell Type

Journal of Virology (2006)

Nathalie J. Arhel Sandie Munier Philippe Souque Karine Mollier Pierre Charneau

We have previously established, using human immunodeficiency virus type 1 (HIV-1) strain LAI, that the HIV-1 central DNA Flap acts as a cis determinant of viral genome nuclear import. Although the impact of the DNA Flap on nuclear import has already found numerous independent confirmations in the context of lentivirus vectors, it has been claimed that it may be nonessential for infectious virus strains LAI, YU-2 (J. D. Dvorin et al., J. Virol. 76:12087-12096, 2002), HXB2, and NL4-3 (A. Limon et al., J. Virol. 76:12078-12086, 2002). We conducted a detailed analysis of virus infectivity using the provirus clones provided by the authors and analogous target cells. In contrast to published data, our results show that all cPPT mutant viruses exhibit reduced infectivity corresponding to a nuclear import defect irrespective of the viral genetic background or target cell.

Provirus

Infectivity

Wild type

10.1128/jvi.00974-06

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Citations (36)

Coordination de la décapsidation et de l’import nucléaire de VIH-1 par la transportine-1

médecine/sciences (2020)

Juliette Fernandez Nathalie J. Arhel

teaching and research institutions in France or abroad, or from public or private research centers.L'archive ouverte pluridisciplinaire HAL, est destinée au dépôt et à la diffusion de documents scientifiques de niveau recherche, publiés ou non, émanant des établissements d'enseignement et de recherche français ou étrangers, des laboratoires publics ou privés.Coordination de la décapsidation et de l'import nucléaire de VIH-1 par la transportine-1

10.1051/medsci/2020031

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Citations (1)

HIV capsid and productive infection: taking steps in the right direction

HAL (Le Centre pour la Communication Scientifique Directe) (2020)

Juliette Fernandez Nathalie J. Arhel

The Human Immunodeficiency Virus Type-1, the causative agent of AIDS, reaches its site of replication by trafficking through the cytoplasm towards the nucleus, benefiting from an active nuclear import through the nuclear pore in order to integrate in the genome of the host cell. Although it is generally accepted that the viral genome remains within the viral capsid for some time after cell entry, the mechanisms responsible for controlled uncoating, which is essential for productive infection, remain poorly understood. Numerous studies now show that the integrity of the viral capsid is essential for transport towards the nucleus, for reverse transcription and nuclear import, and to prevent sensing by innate immune receptors. This review aims to report recent developments in our understanding of the early stages of HIV infection, from entry into the cell to integration, highlighting the cellular partners of the HIV-1 capsid that promote or antagonize infection, as well as the different techniques that are developed for fundamental research and the identification of potential therapeutic targets.

10.1684/vir.2020.0831

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Citations (2)

Measuring the subcellular compartmentalization of viral infections by protein complementation assay

Proceedings of the National Academy of Sciences (2021)

Juliette Fernandez Cédric Hassen‐Khodja Virginie Georget Thierry Rose Yves Jacob

Significance The COVID-19 pandemic has highlighted the need to develop assays that can measure specific steps of viral replication on a large scale. Here we describe an innovative assay called αCentauri that uses fluorescence- or bioluminescence-based protein complementation assays to quantify the subcellular compartmentalization of viruses. As proof of concept, the Centauri fragment was tethered to the nuclear pore complex or sequestered in the nucleus, while the complementary α fragment was attached to the integrase proteins of infectious HIV-1. Thereupon the trafficking of HIV to the nucleus efficiently reconstituted superfolder green fluorescent protein and NanoLuc αCentauri reporters. This technology offers a robust readout of specific steps of viral infection in a multiwell format that is compatible for high-throughput screening.

Compartmentalization (fire protection)

Protein-fragment complementation assay

10.1073/pnas.2010524118

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Citations (4)

Illuminating the nanoscopic world of viruses by fluorescence super-resolution microscopy

Virologie (2021)

Coline Arone Rayane Dibsy Kaushik Inamdar Sébastien Lyonnais Nathalie J. Arhel

The recent revolution in optical fluorescence microscopy, supported by the optimization of both spatial resolution and acquisition speed, led to the ability to visualize nano-scaled objects. Currently, the use of a new generation of super-resolution fluorescence microscopes coupled to improved fluorescent probes gives the possibility to study the replicative cycle of viruses in living cells, at the single-virus and molecule level. In this review, after a brief chronological description of these new approaches, we highlight several examples of super-resolution microscopies that have allowed to revisit our understanding of several human viruses and of host-pathogen interactions.

10.1684/vir.2021.0907

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A new class of capsid-targeting inhibitors that specifically block HIV-1 nuclear import

EMBO Molecular Medicine (2024)

Aude Boulay Emmanuel Quevarec Isabelle Malet Giuseppe Nicastro Célia Chamontin

10.1038/s44321-024-00143-w

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