Nelly Panté

University of British Columbia - Vancouver, Vancouver, British Columbia, Canada

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Publications (69)413.92 Total impact

  • Pierre O Garcin, Ivan R Nabi, Nelly Panté
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    ABSTRACT: Galectin-3 has previously been found to be required by the parvovirus minute virus of mice prototype strain (MVMp) for infection of mouse fibroblast cells. Since MVMp is an oncotropic virus, and galectin-3 is a multifunctional protein implicated in cancer metastasis, we hypothesized that galectin-3 and Mgat5, the Golgi enzyme that synthesizes high-affinity glycan ligands of galectin-3, might play a role in MVMp infection. Using siRNA-mediated knockdown of galectin-3 in mouse cells transformed with polyomavirus middle T antigen and Mgat5(-/-) mouse mammary tumor cells, we found that galectin-3 and Mgat5 are both necessary for efficient MVMp cell entry and infection, but not for cell binding. Moreover, we found that human cancer cells expressing higher levels of galectin-3 were more efficiently infected with MVMp than cell lines expressing lower galectin-3 levels. We conclude that galectin-3 and Mgat5 are involved in MVMp infection, and propose that galectin-3 is a determinant of MVMp oncotropism. Copyright © 2015 Elsevier Inc. All rights reserved.
  • Pierre O. Garcin, Nelly Panté
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    ABSTRACT: The parvovirus minute virus of mice, prototype strain (MVMp), preferentially infects and kills cancer cells. This intrinsic MVMp oncotropism may depend in part on the early stages of MVMp infection. To test this hypothesis, we investigated the early events of MVMp infection in mouse LA9 fibroblasts and a highly invasive mouse mammary tumor cell line derived from polyomavirus middle T antigen-mediated transformation. Using a combination of fluorescence and electron microscopy, we found that various parameters of the cell migration process affect MVMp infection. We show that, after binding to the plasma membrane, MVMp particles rapidly cluster at the leading edge of migrating cells, which exhibit higher levels of MVMp uptake than non-motile cells. Moreover, promoting cell migration on a fibronectin matrix increased MVMp infection, and induction of epithelial–mesenchymal transition allowed MVMp replication in non-permissive epithelial cells. Hence, we propose that cell migration influences the early stages of MVMp infection.
    Virology 11/2014; s 468–470:150–159. DOI:10.1016/j.virol.2014.08.001 · 3.28 Impact Factor
  • Nelly Panté, Birthe Fahrenkrog
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    ABSTRACT: Xenopus oocytes are large in size and perfectly suited for microinjection experiments. Their nuclei, which can be readily isolated manually, are characterized by an extremely high density of nuclear pore complexes (NPCs). Therefore, Xenopus oocytes are an excellent system to study NPC structure and molecular architecture, as well as nucleocytoplasmic transport on an ultrastructural level. A wide range of electron microscopy (EM) techniques can be employed to do so and thin-sectioning immuno-EM has been proven to be a powerful tool in this context. NPCs are composed of multiple copies of a set of about 30 different nucleoporins, which are often large, multidomain proteins. Their complex organization within NPCs can be unraveled by using domain-specific antibodies to individual nucleoporins in combination with microinjection and expression of epitope-tagged nucleoporins. Here, we describe the immuno-EM methods using Xenopus oocyte that allow for precise ultrastructural localization of nucleoporins within the structure of the NPC.
    Methods in cell biology 01/2014; 122C:81-98. DOI:10.1016/B978-0-12-417160-2.00004-7 · 1.44 Impact Factor
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    ABSTRACT: Disassembly of the nuclear lamina is essential in mitosis and apoptosis requiring multiple coordinated enzymatic activities in nucleus and cytoplasm. Activation and coordination of the different activities is poorly understood and moreover complicated as some factors translocate between cytoplasm and nucleus in preparatory phases. Here we used the ability of parvoviruses to induce nuclear membrane breakdown to understand the triggers of key mitotic enzymes. Nuclear envelope disintegration was shown upon infection, microinjection but also upon their application to permeabilized cells. The latter technique also showed that nuclear envelope disintegration was independent upon soluble cytoplasmic factors. Using time-lapse microscopy, we observed that nuclear disassembly exhibited mitosis-like kinetics and occurred suddenly, implying a catastrophic event irrespective of cell- or type of parvovirus used. Analyzing the order of the processes allowed us to propose a model starting with direct binding of parvoviruses to distinct proteins of the nuclear pore causing structural rearrangement of the parvoviruses. The resulting exposure of domains comprising amphipathic helices was required for nuclear envelope disintegration, which comprised disruption of inner and outer nuclear membrane as shown by electron microscopy. Consistent with Ca(++) efflux from the lumen between inner and outer nuclear membrane we found that Ca(++) was essential for nuclear disassembly by activating PKC. PKC activation then triggered activation of cdk-2, which became further activated by caspase-3. Collectively our study shows a unique interaction of a virus with the nuclear envelope, provides evidence that a nuclear pool of executing enzymes is sufficient for nuclear disassembly in quiescent cells, and demonstrates that nuclear disassembly can be uncoupled from initial phases of mitosis.
    PLoS Pathogens 10/2013; 9(10):e1003671. DOI:10.1371/journal.ppat.1003671 · 8.06 Impact Factor
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    Nikta Fay, Nelly Panté
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    ABSTRACT: Intermediate filaments (IFs) have recently been shown to serve novel roles during infection by many viruses. Here we have begun to study the role of IFs during the early steps of infection by the parvovirus minute virus of mice (MVM). We found that during early infection with MVM, after endosomal escape, the vimentin IF network was considerably altered, yielding collapsed immunofluorescence staining near the nuclear periphery. Furthermore, we found that vimentin plays an important role in the life cycle of MVM. The number of cells, which successfully replicated MVM, was reduced in infected cells in which the vimentin network was genetically or pharmacologically modified; viral endocytosis, however, remained unaltered. Perinuclear accumulation of MVM-containing vesicles was reduced in cells lacking vimentin. Our data suggests that vimentin is required for the MVM life cycle, presenting possibly a dual role: (1) following MVM escape from endosomes and (2) during endosomal trafficking of MVM.
    Virology 07/2013; DOI:10.1016/j.virol.2013.06.009 · 3.28 Impact Factor
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    Shelly Au, Wei Wu, Nelly Panté
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    ABSTRACT: Baculoviruses are one of the largest viruses that replicate in the nucleus of their host cells. During infection, the rod-shape, 250-nm long nucleocapsid delivers its genome into the nucleus. Electron microscopy evidence suggests that baculoviruses, specifically the Alphabaculoviruses (nucleopolyhedroviruses) and the Betabaculoviruses (granuloviruses), have evolved two very distinct modes for doing this. Here we review historical and current experimental results of baculovirus nuclear import studies, with an emphasis on electron microscopy studies employing the prototypical baculovirus Autographa californica multiple nucleopolyhedrovirus infecting cultured cells. We also discuss the implications of recent studies towards theories of nuclear transport mechanisms.
    Viruses 07/2013; 5(7):1885-900. DOI:10.3390/v5071885 · 3.28 Impact Factor
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    ABSTRACT: Cellular factors associated with the parvovirus minute virus of mice (MVM) during infection are thought to play important roles in the MVM life cycle but only a few of these have been identified. Here we used a proteomic-based approach in order to identify host-binding partners of MVM. Using purified MVM as bait for immunoprecipitation assays, a total of 150 proteins were identified in MVM immunoprecipitates by quantitative liquid chromatography-tandem mass spectrometry. Galectin-3 was one of six proteins showing a statistically significant enrichment across replicates. Small interfering RNA depletion studies revealed an important role for Galectin-3 in MVM endocytosis and infectivity in LA9 mouse fibroblast cells. Galectin-3-depleted cells were less susceptible to MVM infection than control cells and showed a significant reduction of MVM cellular uptake, but not of MVM binding to the cell surface. Our results indicate an important role for Galectin-3 in the cellular uptake of MVM. We propose that Galectin-3 facilitates the access of MVM to its receptor(s) at the plasma membrane and in this way promotes MVM endocytosis.
    Journal of proteomics 12/2012; DOI:10.1016/j.jprot.2012.12.010 · 5.07 Impact Factor
  • Wei Wu, Nelly Pante
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    ABSTRACT: Background: Influenza A virus poses a serious threat to world public health, particularly the pandemic H1N1 and avian H5N1. Currently, the major anti-influenza strategies are vaccination and antiviral drugs. However, both of these approaches target structural components of the virus which undergo mutation and become resistant to these antiviral approaches. An alternative way to inhibit influenza infection is to interfere with the viral entry into the nucleus, since this process is necessary for viral replication. So far, there are at least two stretches of amino acids sequences located on influenza nucleoprotein (NP) that are know to mediate the nuclear import of the viral ribonucleoproteins (vRNPs) containing the viral genome: NLS1 at the N-terminus of NP, and NLS2 spanning residues 198-216. Sequence allignment shows both NLSs on NP are highly conserved between different strains of influenza A, suggesting that NLSs are ideal candidate for novel antiviral approaches. Methods: To assess this, we are first defining the contribution of the NLSs of NP to nuclear import. The functional role of NLS1 has been very well characterized in previous studies. The specific role of the NLS2 is, however, ill-defined. In our study, we generated chimeric protein by fusing NLS1 or NLS2 to a heterologous protein and characterize the contribution of these NLSs to nuclear import. To analyzed the contribution of the NLS2’s basic amino acids to the nuclear import of the chimera protein, we did site-directed mutagenesis towards NLS2 in chimeric protein. Further analyzation of NLSs's antiviral function was performed by competition assay. Results: Our results showed that NLS2 renders a weak nuclear import behavior compared to NLS1. Interestingly, with only one basic amino acid difference (lysine to arginine) the NLS2 of seasonal flu (H1N1 and H5N1) contributes stronger to the nuclear import of the chimera protein than the NLS2 from pandemic H1N1 and avian H5N1. Using site-directed mutagenesis we further analyzed the contribution of the NLS2’s basic amino acids to the nuclear import of the chimera protein. Our results suggest that NLS2 from pandemic H1N1 and avian H5N1 function as a classical bipartite NLS. However, NLS2 from seasonal flu (H1N1 and H5N1) behaves as a monopartite NLS instead of a bipartite NLS. By performing competition assays using NLS1 and NLS2 chimeras in infected cells, we found that the competing NLSs were able to successfully delayed infection of influenza A virus. Conclusions: NLS2 showed strain-dependent function in nuclear import and contributed less comparing to NLS1. Competition assay results clearly indicate that a good strategy to employ in the development of new influenza antiviral drugs is to interfere with the function of NLSs of influenza NP.
    American Association for the Advancement of Science 2012 Annual Meeting; 02/2012
  • Sarah Cohen, Igor Etingov, Nelly Panté
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    ABSTRACT: The nuclear envelope (NE) is a vital structure that separates the nucleus from the cytoplasm. Because the NE is such a critical cellular barrier, many viral pathogens have evolved to modulate its permeability. They do this either by breaching the NE or by disrupting the integrity and functionality of the nuclear pore complex (NPC). Viruses modulate NE permeability for different reasons. Some viruses disrupt NE to deliver the viral genome into the nucleus for replication, while others cause NE disruption during nuclear egress of newly assembled capsids. Yet, other viruses modulate NE permeability and affect the compartmentalization of host proteins or block the nuclear transport of host proteins involved in the host antiviral response. Recent scientific advances demonstrated that other viruses use proteins of the NPC for viral assembly or disassembly. Here we review the ways in which various viruses affect NE and NPC during infection.
    International review of cell and molecular biology 01/2012; 299:117-59. DOI:10.1016/B978-0-12-394310-1.00003-5 · 4.52 Impact Factor
  • Shelly Au, Nelly Panté
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    ABSTRACT: Baculoviruses are one of the largest viruses that replicate in the nucleus of their host cells. During an infection the capsid, containing the DNA viral genome, is released into the cytoplasm and delivers the genome into the nucleus by a mechanism that is largely unknown. Here, we used capsids of the baculovirus Autographa californica multiple nucleopolyhedrovirus in combination with electron microscopy and discovered this capsid crosses the NPC and enters into the nucleus intact, where it releases its genome. To better illustrate the existence of this capsid through the NPC in its native conformation, we reconstructed the nuclear import event using electron tomography. In addition, using different experimental conditions, we were able to visualize the intact capsid interacting with NPC cytoplasmic filaments, as an initial docking site, and midway through the NPC. Our data suggests the NPC central channel undergoes large-scale rearrangements to allow translocation of the intact 250-nm long baculovirus capsid. We discuss our results in the light of the hypothetical models of NPC function.
    Journal of Structural Biology 11/2011; 177(1):90-8. DOI:10.1016/j.jsb.2011.11.006 · 3.37 Impact Factor
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    ABSTRACT: A hallmark of HIV type 1 and other lentiviruses is their ability to infect and replicate in nondividing cells by commandeering host nuclear transport factors. During the early stages of infection, this is expected to permit the safe passage of viral preintegration complexes (PICs) through nuclear pores. Numerous nuclear transport factors have been identified as essential for HIV-1 infection by genome-wide small interfering RNA screens, and many of these are currently under investigation. Here, using knockdown studies, Matreyek and Engelman further characterize the importance of transportin-3 and nuclear pore complex component nucleoporin 153 for the early stages of HIV-1 infection and show that these two proteins operate synergistically. Also, as was previously observed for transportin-3, they show that the requirement of nucleoporin 153 for PIC nuclear entry is determined by the HIV-1 Capsid protein. The refinement of the list of key nuclear pore complex and transport proteins required for PIC entry, along with a better understanding of the specific mechanisms employed, will undoubtedly lead to the development of future antiretroviral therapies that will have the potential to block HIV-1 viral DNA integration.
    Future Microbiology 11/2011; 6(11):1247-50. DOI:10.2217/fmb.11.111 · 4.02 Impact Factor
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    ABSTRACT: Protozoan parasites, such as Leishmania, still pose an enormous public health problem in many countries throughout the world. Current measures are outdated and have some associated drug resistance, prompting the search into novel therapies. Several innovative approaches are under investigation, including the utilization of host defence peptides (HDPs) as emerging anti-parasitic therapies. HDPs are characterised by their small size, amphipathic nature and cationicity, which induce permeabilization of cell membranes, whilst modulating the immune response of the host. Recently, members of the cathelicidin family of HDPs have demonstrated significant antimicrobial activities against various parasites including Leishmania. The cathelicidin bovine myeloid antimicrobial peptide 28 (BMAP-28) has broad antimicrobial activities and confers protection in animal models of bacterial infection or sepsis. We tested the effectiveness of the use of BMAP-28 and two of its isomers the D-amino acid form (D-BMAP-28) and the retro-inverso form (RI-BMAP-28), as anti-leishmanial agents against the promastigote and amastigote intracellular Leishmania major lifecycle stages. An MTS viability assay was utilized to show the potent antiparasitic activity of BMAP-28 and its protease resistant isomers against L. major promastigotes in vitro. Cell membrane permeability assays, caspase 3/7, Tunel assays and morphologic studies suggested that this was a late stage apoptotic cell death with early osmotic cell lysis caused by the antimicrobial peptides. Furthermore, BMAP-28 and its isomers demonstrated anti-leishmanial activities against intracellular amastigotes within a macrophage infection model. Interestingly, D-BMAP-28 appears to be the most potent antiparasitic of the three isomers against wild type L. major promastigotes and amastigotes. These exciting results suggest that BMAP-28 and its protease resistant isomers have significant therapeutic potential as novel anti-leishmanials.
    PLoS Neglected Tropical Diseases 05/2011; 5(5):e1141. DOI:10.1371/journal.pntd.0001141 · 4.49 Impact Factor
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    ABSTRACT: Human immunodeficiency virus type 1 (HIV-1) commandeers host cell proteins and machineries for its replication. Our earlier work showed that HIV-1 induced the cytoplasmic retention of nucleocytoplasmic shuttling and ribonucleic acid (RNA)-binding proteins. This retention is dependent on nuclear export of the viral genomic RNA and on changes in the localization and expression level of the nucleoporin (Nup) p62 (Nup62). To further characterize the extent of perturbation induced by HIV-1, we performed proteomics analyses of nuclear envelopes (NEs) isolated from infected T cells. Infection induced extensive changes in the composition of the NE and its associated proteins, including a remarkable decrease in the abundance of Nups. Immunogold electron microscopy revealed the translocation of Nups into the cytoplasm. Nup62 was identified as a component of purified virus, and small interfering RNA depletion studies revealed an important role for this Nup in virus gene expression and infectivity. This detailed analysis highlights the profound effects on NE composition induced by HIV-1 infection, providing further evidence of the magnitude of viral control over the cell biology of its host.
    The Journal of Cell Biology 05/2011; 193(4):619-31. DOI:10.1083/jcb.201008064 · 9.69 Impact Factor
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    ABSTRACT: Parvoviruses are small, nonenveloped, single-stranded DNA viruses which replicate in the nucleus of the host cell. We have previously found that early during infection the parvovirus minute virus of mice (MVM) causes small, transient disruptions of the nuclear envelope (NE). We have now investigated the mechanism used by MVM to disrupt the NE. Here we show that the viral phospholipase A2, the only known enzymatic domain on the parvovirus capsid, is not involved in causing NE disruption. Instead, the virus utilizes host cell caspases, which are proteases involved in causing NE breakdown during apoptosis, to facilitate these nuclear membrane disruptions. Studies with pharmacological inhibitors indicate that caspase-3 in particular is involved. A caspase-3 inhibitor prevents nuclear lamin cleavage and NE disruption in MVM-infected mouse fibroblast cells and reduces nuclear entry of MVM capsids and viral gene expression. Caspase-3 is, however, not activated above basal levels in MVM-infected cells, and other aspects of apoptosis are not triggered during early MVM infection. Instead, basally active caspase-3 is relocalized to the nuclei of infected cells. We propose that NE disruption involving caspases plays a role in (i) parvovirus entry into the nucleus and (ii) alteration of the compartmentalization of host proteins in a way that is favorable for the virus.
    Journal of Virology 03/2011; 85(10):4863-74. DOI:10.1128/JVI.01999-10 · 4.65 Impact Factor
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    Sarah Cohen, Shelly Au, Nelly Panté
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    ABSTRACT: Many viruses depend on nuclear proteins for replication. Therefore, their viral genome must enter the nucleus of the host cell. In this review we briefly summarize the principles of nucleocytoplasmic transport, and then describe the diverse strategies used by viruses to deliver their genomes into the host nucleus. Some of the emerging mechanisms include: (1) nuclear entry during mitosis, when the nuclear envelope is disassembled, (2) viral genome release in the cytoplasm followed by entry of the genome through the nuclear pore complex (NPC), (3) capsid docking at the cytoplasmic side of the NPC, followed by genome release, (4) nuclear entry of intact capsids through the NPC, followed by genome release, and (5) nuclear entry via virus-induced disruption of the nuclear envelope. Which mechanism a particular virus uses depends on the size and structure of the virus, as well as the cellular cues used by the virus to trigger capsid disassembly and genome release. This article is part of a Special Issue entitled: Regulation of Signaling and Cellular Fate through Modulation of Nuclear Protein Import.
    Biochimica et Biophysica Acta 12/2010; 1813(9):1634-45. DOI:10.1016/j.bbamcr.2010.12.009 · 4.66 Impact Factor
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    Lixin Zhou, Nelly Panté
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    ABSTRACT: Nucleoporin 153 (Nup153), a component of the nuclear pore complex (NPC), has been implicated in the interaction of the NPC with the nuclear lamina. Here we show that depletion of Nup153 by RNAi results in alteration of the organization of the nuclear lamina and the nuclear lamin-binding protein Sun1. More striking, Nup153 depletion induces a dramatic cytoskeletal rearrangement that impairs cell migration in human breast carcinoma cells. Our results point to a very prominent role of Nup153 in connection to cell motility that could be exploited in order to develop novel anti-cancer therapy.
    FEBS letters 07/2010; 584(14):3013-20. DOI:10.1016/j.febslet.2010.05.038 · 3.54 Impact Factor
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    ABSTRACT: Importin beta mediates active passage of cellular substrates through the nuclear pore complex (NPC). Adaptors such as importin alpha and snurportin associate with importin beta via an importin beta binding (IBB) domain. The intrinsic structural flexibility of importin beta allows its concerted interactions with IBB domains, phenylalanine-glycine nucleoporins, and the GTPase Ran during transport. In this paper, we provide evidence that the nature of the IBB domain modulates the affinity of the import complex for the NPC. In permeabilized cells, importin beta imports a cargo fused to the snurportin IBB (sIBB) with approximately 70% reduced energy requirement as compared with the classical importin alpha IBB. At the molecular level, this is explained by approximately 200-fold reduced affinity of importin beta for Nup62, when bound to the sIBB. Consistently, in vivo, the importin beta.sIBB complex has greatly reduced persistence inside the central channel of the NPC. We propose that by controlling the degree of strain in the tertiary structure of importin beta, the IBB domain modulates the affinity of the import complex for nucleoporins, thus dictating its persistence inside the NPC.
    Journal of Biological Chemistry 03/2010; 285(18):13769-80. DOI:10.1074/jbc.M109.095760 · 4.60 Impact Factor
  • Shelly Au, Sarah Cohen, Nelly Panté
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    ABSTRACT: Microinjection of Xenopus laevis oocytes is an excellent system for studying nuclear transport because of the large size of the oocyte and its high nuclear pore complex (NPC) density. In addition, the fact that Xenopus oocytes are not permissive for most mammalian viruses makes this system especially useful for studying nuclear transport of viruses in the absence of the confounding factor of virus replication. In this article, we briefly discuss the contribution of microinjection of Xenopus oocytes to the field of nuclear transport. We then describe the protocols we have developed using microinjection of Xenopus oocytes to study nuclear transport of viral capsids, and summarize variations of the technique that can be used to address many different questions about the nuclear transport of viruses.
    Methods 02/2010; 51(1):114-20. DOI:10.1016/j.ymeth.2010.02.001 · 3.22 Impact Factor
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    ABSTRACT: Virtually all DNA viruses including hepatitis B viruses (HBV) replicate their genome inside the nucleus. In non-dividing cells, the genome has to pass through the nuclear pore complexes (NPCs) by the aid of nuclear transport receptors as e.g. importin beta (karyopherin). Most viruses release their genome in the cytoplasm or at the cytosolic face of the NPC, as the diameter of their capsids exceeds the size of the NPC. The DNA genome of HBV is derived from reverse transcription of an RNA pregenome. Genome maturation occurs in cytosolic capsids and progeny capsids can deliver the genome into the nucleus causing nuclear genome amplification. The karyophilic capsids are small enough to pass the NPC, but nuclear entry of capsids with an immature genome is halted in the nuclear basket on the nuclear side of the NPC, and the genome remains encapsidated. In contrast, capsids with a mature genome enter the basket and consequently liberate the genome. Investigating the difference between immature and mature capsids, we found that mature capsids had to disintegrate in order to leave the nuclear basket. The arrest of a karyophilic cargo at the nuclear pore is a rare phenomenon, which has been described for only very few cellular proteins participating in nuclear entry. We analyzed the interactions causing HBV capsid retention. By pull-down assays and partial siRNA depletion, we showed that HBV capsids directly interact with nucleoporin 153 (Nup153), an essential protein of the nuclear basket which participates in nuclear transport via importin beta. The binding sites of importin beta and capsids were shown to overlap but capsid binding was 150-fold stronger. In cellulo experiments using digitonin-permeabilized cells confirmed the interference between capsid binding and nuclear import by importin beta. Collectively, our findings describe a unique nuclear import strategy not only for viruses but for all karyophilic cargos.
    PLoS Pathogens 01/2010; 6(1):e1000741. DOI:10.1371/journal.ppat.1000741 · 8.06 Impact Factor
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    ABSTRACT: The rise of antibiotic resistant pathogens is one of the most pressing global health issues. Discovery of new classes of antibiotics has not kept pace; new agents often suffer from cross-resistance to existing agents of similar structure. Short, cationic peptides with antimicrobial activity are essential to the host defenses of many organisms and represent a promising new class of antimicrobials. This paper reports the successful in silico screening for potent antibiotic peptides using a combination of QSAR and machine learning techniques. On the basis of initial high-throughput measurements of activity of over 1400 random peptides, artificial neural network models were built using QSAR descriptors and subsequently used to screen an in silico library of approximately 100,000 peptides. In vitro validation of the modeling showed 94% accuracy in identifying highly active peptides. The best peptides identified through screening were found to have activities comparable or superior to those of four conventional antibiotics and superior to the peptide most advanced in clinical development against a broad array of multiresistant human pathogens.
    Journal of Medicinal Chemistry 05/2009; 52(7):2006-15. DOI:10.1021/jm8015365 · 5.48 Impact Factor

Publication Stats

4k Citations
413.92 Total Impact Points


  • 2003–2014
    • University of British Columbia - Vancouver
      • Department of Zoology
      Vancouver, British Columbia, Canada
  • 2013
    • French National Centre for Scientific Research
      Lutetia Parisorum, Île-de-France, France
  • 2009–2011
    • Lady Davis Institute for Medical Research
      Montréal, Quebec, Canada
  • 2002
    • Justus-Liebig-Universität Gießen
      Gieben, Hesse, Germany
  • 2000
    • The University of Calgary
      Calgary, Alberta, Canada
    • Eawag: Das Wasserforschungs-Institut des ETH-Bereichs
      Duebendorf, Zurich, Switzerland
  • 1994–2000
    • Universität Basel
      • Department of Biophysical Chemistry
      Bâle, Basel-City, Switzerland
  • 1999
    • ETH Zurich
      • Institute of Biochemistry
      Zürich, ZH, Switzerland
  • 1995
    • The Scripps Research Institute
      • Department of Cell and Molecular Biology
      La Jolla, CA, United States
    • Nagoya University
      • Division of Cell Science
      Nagoya-shi, Aichi-ken, Japan
  • 1994–1995
    • Johns Hopkins University
      • Department of Cell Biology
      Baltimore, Maryland, United States