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  • 1
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    Ebola virus entry requires the cholesterol transporter Niemann-Pick C1 (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-08-26
    Description: Infections by the Ebola and Marburg filoviruses cause a rapidly fatal haemorrhagic fever in humans for which no approved antivirals are available. Filovirus entry is mediated by the viral spike glycoprotein (GP), which attaches viral particles to the cell surface, delivers them to endosomes and catalyses fusion between viral and endosomal membranes. Additional host factors in the endosomal compartment are probably required for viral membrane fusion; however, despite considerable efforts, these critical host factors have defied molecular identification. Here we describe a genome-wide haploid genetic screen in human cells to identify host factors required for Ebola virus entry. Our screen uncovered 67 mutations disrupting all six members of the homotypic fusion and vacuole protein-sorting (HOPS) multisubunit tethering complex, which is involved in the fusion of endosomes to lysosomes, and 39 independent mutations that disrupt the endo/lysosomal cholesterol transporter protein Niemann-Pick C1 (NPC1). Cells defective for the HOPS complex or NPC1 function, including primary fibroblasts derived from human Niemann-Pick type C1 disease patients, are resistant to infection by Ebola virus and Marburg virus, but remain fully susceptible to a suite of unrelated viruses. We show that membrane fusion mediated by filovirus glycoproteins and viral escape from the vesicular compartment require the NPC1 protein, independent of its known function in cholesterol transport. Our findings uncover unique features of the entry pathway used by filoviruses and indicate potential antiviral strategies to combat these deadly agents.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3175325/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3175325/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carette, Jan E -- Raaben, Matthijs -- Wong, Anthony C -- Herbert, Andrew S -- Obernosterer, Gregor -- Mulherkar, Nirupama -- Kuehne, Ana I -- Kranzusch, Philip J -- Griffin, April M -- Ruthel, Gordon -- Dal Cin, Paola -- Dye, John M -- Whelan, Sean P -- Chandran, Kartik -- Brummelkamp, Thijn R -- AI081842/AI/NIAID NIH HHS/ -- R01 AI081842/AI/NIAID NIH HHS/ -- R01 AI081842-03/AI/NIAID NIH HHS/ -- R01 AI088027/AI/NIAID NIH HHS/ -- R01 AI088027-03/AI/NIAID NIH HHS/ -- R21 HG004938/HG/NHGRI NIH HHS/ -- R21 HG004938-01/HG/NHGRI NIH HHS/ -- T32 AI070117/AI/NIAID NIH HHS/ -- T32 GM007288/GM/NIGMS NIH HHS/ -- U54 AI057159/AI/NIAID NIH HHS/ -- U54 AI057159-09/AI/NIAID NIH HHS/ -- England -- Nature. 2011 Aug 24;477(7364):340-3. doi: 10.1038/nature10348.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, Massachusetts 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21866103" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Carrier Proteins/genetics/*metabolism ; Cell Line ; Cholesterol/*metabolism ; Ebolavirus/*physiology ; Endosomes/metabolism ; Fibroblasts/metabolism/pathology/virology ; Genome, Human/genetics ; Glycoproteins/metabolism ; Haploidy ; Hemorrhagic Fever, Ebola/drug therapy/metabolism ; Host-Pathogen Interactions/genetics ; Humans ; Lysosomes/metabolism ; Marburg Virus Disease/drug therapy/metabolism ; Marburgvirus/physiology ; Membrane Fusion/genetics/physiology ; Membrane Glycoproteins/deficiency/genetics/*metabolism ; Multiprotein Complexes/chemistry/deficiency/genetics/metabolism ; Mutation/genetics ; Niemann-Pick Diseases/pathology/virology ; Receptors, Virus/metabolism ; Viral Fusion Proteins/metabolism ; *Virus Internalization
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Virus entry. Lassa virus entry requires a trigger-induced receptor switch (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-06-28
    Description: Lassa virus spreads from a rodent to humans and can lead to lethal hemorrhagic fever. Despite its broad tropism, chicken cells were reported 30 years ago to resist infection. We found that Lassa virus readily engaged its cell-surface receptor alpha-dystroglycan in avian cells, but virus entry in susceptible species involved a pH-dependent switch to an intracellular receptor, the lysosome-resident protein LAMP1. Iterative haploid screens revealed that the sialyltransferase ST3GAL4 was required for the interaction of the virus glycoprotein with LAMP1. A single glycosylated residue in LAMP1, present in susceptible species but absent in birds, was essential for interaction with the Lassa virus envelope protein and subsequent infection. The resistance of Lamp1-deficient mice to Lassa virus highlights the relevance of this receptor switch in vivo.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4239993/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4239993/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jae, Lucas T -- Raaben, Matthijs -- Herbert, Andrew S -- Kuehne, Ana I -- Wirchnianski, Ariel S -- Soh, Timothy K -- Stubbs, Sarah H -- Janssen, Hans -- Damme, Markus -- Saftig, Paul -- Whelan, Sean P -- Dye, John M -- Brummelkamp, Thijn R -- AI081842/AI/NIAID NIH HHS/ -- AI109740/AI/NIAID NIH HHS/ -- R01 AI081842/AI/NIAID NIH HHS/ -- T32 AI007245/AI/NIAID NIH HHS/ -- U19 AI109740/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2014 Jun 27;344(6191):1506-10. doi: 10.1126/science.1252480.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX, Amsterdam, Netherlands. ; Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX, Amsterdam, Netherlands. Department of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA. ; U.S. Army Medical Research Institute of Infectious Diseases, 1425 Porter Street, Fort Detrick, MD 21702-5011, USA. ; Department of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA. ; Biochemisches Institut, Christian Albrechts-Universitat Kiel, 24118 Kiel, Germany. ; Department of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA. t.brummelkamp@nki.nl john.m.dye1.civ@mail.mil sean_whelan@hms.harvard.edu. ; U.S. Army Medical Research Institute of Infectious Diseases, 1425 Porter Street, Fort Detrick, MD 21702-5011, USA. t.brummelkamp@nki.nl john.m.dye1.civ@mail.mil sean_whelan@hms.harvard.edu. ; Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX, Amsterdam, Netherlands. CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria. Cancer Genomics Center (CGC.nl), Plesmanlaan 121, 1066 CX, Amsterdam, Netherlands. t.brummelkamp@nki.nl john.m.dye1.civ@mail.mil sean_whelan@hms.harvard.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24970085" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cell Membrane/metabolism/virology ; Cells, Cultured ; Chickens ; Dystroglycans/genetics/metabolism ; Glycosylation ; Humans ; Hydrogen-Ion Concentration ; Lassa Fever/virology ; Lassa virus/*physiology ; Lysosomal-Associated Membrane Protein 1/chemistry/*metabolism ; Lysosomes/metabolism/virology ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Protein Binding ; Receptors, Virus/*metabolism ; Sialyltransferases/metabolism ; Viral Envelope Proteins/*metabolism ; *Virus Internalization
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
    Electronic Resource
    Electronic Resource
    On bidirectional fifth-order nonlinear evolution equations, Lax pairs, and directionally dependent solitary waves (2001)
    College Park, Md. : American Institute of Physics (AIP)
    Journal of Mathematical Physics 42 (2001), S. 2567-2589 
    Details
    ISSN: 1089-7658
    Source: AIP Digital Archive
    Topics: Mathematics , Physics
    Notes: In this paper, Lax pairs are constructed for two fifth-order nonlinear evolution equations of "Boussinesq"-type which govern wave propagation in two opposite directions. One of the equations is related to the well-known Sawada–Kotera (SK) equation and, through its bilinear form, is identified with the Ramani equation. The second equation—about which very little seems to be known—may be considered a bidirectional version of the Kaup–Kupershmidt (KK) equation and is the main focus of this study. The "anomalous" solitary wave of this latter equation is derived and is found to possess the remarkable property that its profile depends on the direction of propagation. This type of directional dependence would appear to be quite unusual and, to our knowledge, has not been reported in the literature before now. By taking an appropriate undirectional (long wave) limit, it is shown that neither the Ramani, nor the bidirectional Kaup–Kupershmidt (bKK) equation can be classified as truly "Boussinesq" in character (a distinction that is made precise in the study). Recursion formulas are given for generating an infinity of conserved densities for both equations. These are used to obtain the first few conservation laws of the bKK and Ramani equations explicitly; not surprisingly, they exhibit the same lacunary behavior as their unidirectional counterparts. In conclusion, a canonical interpretation of the N-soliton solution of the bKK equation is proposed which provides a basis for constructing these anomalous solitons in a future work. © 2001 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.1354642
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  • 4
    Electronic Resource
    Electronic Resource
    An inverse scattering scheme for the regularized long-wave equation (2000)
    College Park, Md. : American Institute of Physics (AIP)
    Journal of Mathematical Physics 41 (2000), S. 2889-2904 
    Details
    ISSN: 1089-7658
    Source: AIP Digital Archive
    Topics: Mathematics , Physics
    Notes: The regularized long-wave (RLW) equation was proposed as an alternative model to the Korteweg–de Vries (KdV) equation to describe small-amplitude long waves in shallow water. However, unlike the KdV equation—which is exactly solvable by the inverse scattering method—the RLW equation is deemed not to be completely integrable. In this paper, an inverse scattering scheme is described for solving the RLW equation which is based on the "dressing method" of Zakharov and Shabat. Significantly, the compatibility of the "dressed" operators leads to two governing equations which, taken together, reduce to the RLW equation. One of these equations links the RLW equation to the (completely integrable) shallow water wave (ASWW) equation due to Ablowitz et al.; the second is a linear wave constraint that signals the nonintegrability of the RLW equation and prohibits the existence of multisoliton solutions. Contrary to results already reported in the literature, the proposed scheme associates the RLW equation with a third-order scattering problem. Moreover, as a special case of the RLW scheme, we obtain an inverse scattering procedure for the integrable ASWW equation; its formulation via the dressing method would appear to be given here for the first time. Explicit solutions are constructed for both equations using the respective inverse scattering schemes. © 2000 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.533278
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  • 5
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    Postexposure antibody prophylaxis protects nonhuman primates from filovirus disease (2012)
    National Academy of Sciences
    Details
    Publication Date: 2012-03-12
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 6
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    A nonreplicating subunit vaccine protects mice against lethal Ebola virus challenge (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-12-05
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 7
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    Polyclonal antibody protects NHPs from filovirus [Medical Sciences] (2012)
    National Academy of Sciences
    Details
    Publication Date: 2012-03-28
    Description: Antibody therapies to prevent or limit filovirus infections have received modest interest in recent years, in part because of early negative experimental evidence. We have overcome the limitations of this approach, leveraging the use of antibody from nonhuman primates (NHPs) that survived challenge to filoviruses under controlled conditions. By using concentrated, polyclonal IgG antibody from these survivors, we treated filovirus-infected NHPs with multiple doses administered over the clinical phase of disease. In the first study, Marburg virus (MARV)-infected NHPs were treated 15 to 30 min postexposure with virus-specific IgG, with additional treatments on days 4 and 8 postexposure. The postexposure IgG treatment was completely protective, with no signs of disease or detectable viremia. MARV-specific IgM antibody responses were generated, and all macaques survived rechallenge with MARV, suggesting that they generated an immune response to virus replication. In the next set of studies, NHPs were infected with MARV or Ebola virus (EBOV), and treatments were delayed 48 h, with additional treatments on days 4 and 8 postexposure. The delayed treatments protected both MARV- and EBOV-challenged NHPs. In both studies, two of the three IgG-treated NHPs had no clinical signs of illness, with the third NHP developing mild and delayed signs of disease followed by full recovery. These studies clearly demonstrate that postexposure antibody treatments can protect NHPs and open avenues for filovirus therapies for human use using established Food and Drug Administration-approved polyclonal or monoclonal antibody technologies.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 8
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    A nonreplicating subunit vaccine protects mice against lethal Ebola virus challenge [Immunology] (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-12-21
    Description: Ebola hemorrhagic fever is an acute and often deadly disease caused by Ebola virus (EBOV). The possible intentional use of this virus against human populations has led to design of vaccines that could be incorporated into a national stockpile for biological threat reduction. We have evaluated the immunogenicity and efficacy of an EBOV vaccine candidate in which the viral surface glycoprotein is biomanufactured as a fusion to a monoclonal antibody that recognizes an epitope in glycoprotein, resulting in the production of Ebola immune complexes (EICs). Although antigen–antibody immune complexes are known to be efficiently processed and presented to immune effector cells, we found that codelivery of the EIC with Toll-like receptor agonists elicited a more robust antibody response in mice than did EIC alone. Among the compounds tested, polyinosinic:polycytidylic acid (PIC, a Toll-like receptor 3 agonist) was highly effective as an adjuvant agent. After vaccinating mice with EIC plus PIC, 80% of the animals were protected against a lethal challenge with live EBOV (30,000 LD50 of mouse adapted virus). Surviving animals showed a mixed Th1/Th2 response to the antigen, suggesting this may be important for protection. Survival after vaccination with EIC plus PIC was statistically equivalent to that achieved with an alternative viral vector vaccine candidate reported in the literature. Because nonreplicating subunit vaccines offer the possibility of formulation for cost-effective, long-term storage in biothreat reduction repositories, EIC is an attractive option for public health defense measures.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 9
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    A bidirectional Kaup–Kupershmidt equation and directionally dependent solitons (2002)
    American Institute of Physics
    Details
    Publication Date: 2002-01-01
    Print ISSN: 0022-2488
    Electronic ISSN: 1089-7658
    Topics: Mathematics , Physics
    Published by American Institute of Physics
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  • 10
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    An inverse scattering scheme for the regularized long-wave equation (2000)
    American Institute of Physics
    Details
    Publication Date: 2000-05-01
    Print ISSN: 0022-2488
    Electronic ISSN: 1089-7658
    Topics: Mathematics , Physics
    Published by American Institute of Physics
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