Acetylcholine Receptors 61 Acid Blob Activator 321 Acquired Immune
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Metagenomic Analysis Indicates That Stressors Induce Production of Herpes-Like Viruses in the Coral Porites Compressa
Metagenomic analysis indicates that stressors induce production of herpes-like viruses in the coral Porites compressa Rebecca L. Vega Thurbera,b,1, Katie L. Barotta, Dana Halla, Hong Liua, Beltran Rodriguez-Muellera, Christelle Desnuesa,c, Robert A. Edwardsa,d,e,f, Matthew Haynesa, Florent E. Anglya, Linda Wegleya, and Forest L. Rohwera,e aDepartment of Biology, dComputational Sciences Research Center, and eCenter for Microbial Sciences, San Diego State University, San Diego, CA 92182; bDepartment of Biological Sciences, Florida International University, 3000 North East 151st, North Miami, FL 33181; cUnite´des Rickettsies, Unite Mixte de Recherche, Centre National de la Recherche Scientifique 6020. Faculte´deMe´ decine de la Timone, 13385 Marseille, France; and fMathematics and Computer Science Division, Argonne National Laboratory, Argonne, IL 60439 Communicated by Baruch S. Blumberg, Fox Chase Cancer Center, Philadelphia, PA, September 11, 2008 (received for review April 25, 2008) During the last several decades corals have been in decline and at least established, an increase in viral particles within dinoflagellates has one-third of all coral species are now threatened with extinction. been hypothesized to be responsible for symbiont loss during Coral disease has been a major contributor to this threat, but little is bleaching (25–27). VLPs also have been identified visually on known about the responsible pathogens. To date most research has several species of scleractinian corals, specifically: Acropora muri- focused on bacterial and fungal diseases; however, viruses may also cata, Porites lobata, Porites lutea, and Porites australiensis (28). Based be important for coral health. Using a combination of empirical viral on morphological characteristics, these VLPs belong to several viral metagenomics and real-time PCR, we show that Porites compressa families including: tailed phages, large filamentous, and small corals contain a suite of eukaryotic viruses, many related to the (30–80 nm) to large (Ͼ100 nm) polyhedral viruses (29). -
How Influenza Virus Uses Host Cell Pathways During Uncoating
cells Review How Influenza Virus Uses Host Cell Pathways during Uncoating Etori Aguiar Moreira 1 , Yohei Yamauchi 2 and Patrick Matthias 1,3,* 1 Friedrich Miescher Institute for Biomedical Research, 4058 Basel, Switzerland; [email protected] 2 Faculty of Life Sciences, School of Cellular and Molecular Medicine, University of Bristol, Bristol BS8 1TD, UK; [email protected] 3 Faculty of Sciences, University of Basel, 4031 Basel, Switzerland * Correspondence: [email protected] Abstract: Influenza is a zoonotic respiratory disease of major public health interest due to its pan- demic potential, and a threat to animals and the human population. The influenza A virus genome consists of eight single-stranded RNA segments sequestered within a protein capsid and a lipid bilayer envelope. During host cell entry, cellular cues contribute to viral conformational changes that promote critical events such as fusion with late endosomes, capsid uncoating and viral genome release into the cytosol. In this focused review, we concisely describe the virus infection cycle and highlight the recent findings of host cell pathways and cytosolic proteins that assist influenza uncoating during host cell entry. Keywords: influenza; capsid uncoating; HDAC6; ubiquitin; EPS8; TNPO1; pandemic; M1; virus– host interaction Citation: Moreira, E.A.; Yamauchi, Y.; Matthias, P. How Influenza Virus Uses Host Cell Pathways during 1. Introduction Uncoating. Cells 2021, 10, 1722. Viruses are microscopic parasites that, unable to self-replicate, subvert a host cell https://doi.org/10.3390/ for their replication and propagation. Despite their apparent simplicity, they can cause cells10071722 severe diseases and even pose pandemic threats [1–3]. -
On the Biological Success of Viruses
MI67CH25-Turner ARI 19 June 2013 8:14 V I E E W R S Review in Advance first posted online on June 28, 2013. (Changes may still occur before final publication E online and in print.) I N C N A D V A On the Biological Success of Viruses Brian R. Wasik and Paul E. Turner Department of Ecology and Evolutionary Biology, Yale University, New Haven, Connecticut 06520-8106; email: [email protected], [email protected] Annu. Rev. Microbiol. 2013. 67:519–41 Keywords The Annual Review of Microbiology is online at adaptation, biodiversity, environmental change, evolvability, extinction, micro.annualreviews.org robustness This article’s doi: 10.1146/annurev-micro-090110-102833 Abstract Copyright c 2013 by Annual Reviews. Are viruses more biologically successful than cellular life? Here we exam- All rights reserved ine many ways of gauging biological success, including numerical abun- dance, environmental tolerance, type biodiversity, reproductive potential, and widespread impact on other organisms. We especially focus on suc- cessful ability to evolutionarily adapt in the face of environmental change. Viruses are often challenged by dynamic environments, such as host immune function and evolved resistance as well as abiotic fluctuations in temperature, moisture, and other stressors that reduce virion stability. Despite these chal- lenges, our experimental evolution studies show that viruses can often readily adapt, and novel virus emergence in humans and other hosts is increasingly problematic. We additionally consider whether viruses are advantaged in evolvability—the capacity to evolve—and in avoidance of extinction. On the basis of these different ways of gauging biological success, we conclude that viruses are the most successful inhabitants of the biosphere. -
Ebolaviruses: New Roles for Old Proteins
REVIEW Ebolaviruses: New roles for old proteins Diego Cantoni, Jeremy S. Rossman* School of Biosciences, University of Kent, Canterbury, United Kingdom * [email protected] Abstract In 2014, the world witnessed the largest Ebolavirus outbreak in recorded history. The subse- quent humanitarian effort spurred extensive research, significantly enhancing our under- standing of ebolavirus replication and pathogenicity. The main functions of each ebolavirus protein have been studied extensively since the discovery of the virus in 1976; however, the recent expansion of ebolavirus research has led to the discovery of new protein functions. a1111111111 These newly discovered roles are revealing new mechanisms of virus replication and patho- a1111111111 genicity, whilst enhancing our understanding of the broad functions of each ebolavirus viral a1111111111 a1111111111 protein (VP). Many of these new functions appear to be unrelated to the protein's primary a1111111111 function during virus replication. Such new functions range from bystander T-lymphocyte death caused by VP40-secreted exosomes to new roles for VP24 in viral particle formation. This review highlights the newly discovered roles of ebolavirus proteins in order to provide a more encompassing view of ebolavirus replication and pathogenicity. OPEN ACCESS Citation: Cantoni D, Rossman JS (2018) Ebolaviruses: New roles for old proteins. PLoS Negl Trop Dis 12(5): e0006349. https://doi.org/ Author summary 10.1371/journal.pntd.0006349 Between 2014 and 2016, West Africa experienced the largest Ebolavirus outbreak in Editor: Patricia V. Aguilar, University of Texas recorded history. The international containment effort spurred extensive research that is Medical Branch, UNITED STATES enhancing our understanding of ebolavirus replication and pathogenicity. -
The Complete Genome of an Endogenous Nimavirus (Nimav-1 Lva) from the Pacific Whiteleg Shrimp Penaeus (Litopenaeus) Vannamei
G C A T T A C G G C A T genes Article The Complete Genome of an Endogenous Nimavirus (Nimav-1_LVa) From the Pacific Whiteleg Shrimp Penaeus (Litopenaeus) Vannamei Weidong Bao 1,* , Kathy F. J. Tang 2 and Acacia Alcivar-Warren 3,4,* 1 Genetic Information Research Institute, 20380 Town Center Lane, Suite 240, Cupertino, CA 95014, USA 2 Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, 106 Nanjing Road, Qingdao 266071, China; [email protected] 3 Fundación para la Conservation de la Biodiversidad Acuática y Terrestre (FUCOBI), Quito EC1701, Ecuador 4 Environmental Genomics Inc., ONE HEALTH Epigenomics Educational Initiative, P.O. Box 196, Southborough, MA 01772, USA * Correspondence: [email protected] (W.B.); [email protected] (A.A.-W.) Received: 17 December 2019; Accepted: 9 January 2020; Published: 14 January 2020 Abstract: White spot syndrome virus (WSSV), the lone virus of the genus Whispovirus under the family Nimaviridae, is one of the most devastating viruses affecting the shrimp farming industry. Knowledge about this virus, in particular, its evolution history, has been limited, partly due to its large genome and the lack of other closely related free-living viruses for comparative studies. In this study, we reconstructed a full-length endogenous nimavirus consensus genome, Nimav-1_LVa (279,905 bp), in the genome sequence of Penaeus (Litopenaeus) vannamei breed Kehai No. 1 (ASM378908v1). This endogenous virus seemed to insert exclusively into the telomeric pentanucleotide microsatellite (TAACC/GGTTA)n. It encoded 117 putative genes, with some containing introns, such as g012 (inhibitor of apoptosis, IAP), g046 (crustacean hyperglycemic hormone, CHH), g155 (innexin), g158 (Bax inhibitor 1 like). -
JOURNAL of VIROLOGY VOLUME 57 * MARCH 1986 * NUMBER 3 Arnold J
JOURNAL OF VIROLOGY VOLUME 57 * MARCH 1986 * NUMBER 3 Arnold J. Levine, Editor in Chief Michael B. A. Oldstone, Editor (1988) (1989) Scripps Clinic & Research Foundation Princeton University La Jolla, Calif. Princeton, N.J. Thomas E. Shenk, Editor (1989) David T. Denhardt, Editor (1987) Princeton University University of Western Ontario Princeton, N.J. London, Ontario, Canada Anna Marie Skalka, Editor (1989) Bernard N. Fields, Editor (1988) Hoffmann-La Roche Inc. Harvard Medical School Nutley, N.J. Boston, Mass. Robert A. Weisberg, Editor (1988) Robert M. Krug, Editor (1987) National Institute of Child Health Sloan-Kettering Institute and Human Development New York, N.Y. Bethesda, Md. EDITORIAL BOARD James Alwine (1988) Hidesaburo Hanafusa (1986) Lois K. Miller (1988) Priscilla A. Schaffer (1987) David Baltimore (1987) William S. Hayward (1987) Peter Model (1986) Sondra Schlesinger (1986) Tamar Ben-Porat (1987) Roger Hendrix (1987) Bernard Moss (1986) Manfred Schubert (1988) Kenneth I. Berns (1988) Martin Hirsch (1986) Fred Murphy (1986) June R. Scott (1986) Michael Botchan (1986) John J. Holland (1987) Opendra Narayan (1988) Bart Sefton (1988) Thomas J. Braciale (1988) Ian H. Holmes (1986) Joseph R. Nevins (1988) Charles J. Sherr (1987) Joan Brugge (1988) Robert W. Honess (1986) Nancy G. Nossal (1987) Saul J. Silverstein Barrie J. Carter (1987) Nancy Hopkins (1986) Abner Notkins (1986) (1988) John M. Coffin (1986) Peter M. Howley (1987) J. Thomas Parsons (1986) Patricia G. Spear (1987) Geoffrey M. Cooper (1987) Alice S. Huang (1987) Ulf G. Pettersson (1986) Nat Sternberg (1986) Donald Court (1987) Steve Hughes (1988) Lennart Philipson (1987) Bruce Stillman (1988) Richard Courtney (1986) Tony Hunter (1986) Lewis I. -
A Novel RNA Virus in the Parasitoid Wasp Lysiphlebus Fabarum: Genomic Structure, Prevalence, and Transmission
viruses Article A Novel RNA Virus in the Parasitoid Wasp Lysiphlebus fabarum: Genomic Structure, Prevalence, and Transmission 1,2, , 1,2 1,2, Martina N. Lüthi * y , Christoph Vorburger and Alice B. Dennis z 1 Institute of Integrative Biology, ETH Zürich, Universitätstrasse 16, 8092 Zürich, Switzerland; [email protected] (C.V.); [email protected] (A.B.D.) 2 Eawag, Swiss Federal Institute of Aquatic Science and Technology, Überlandstrasse 133, 8600 Dübendorf, Switzerland * Correspondence: [email protected] Current address: Institute of Plant Sciences, University of Bern, Altenbergrain 21, 3013 Bern, Switzerland. y Current address: Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Strasse z 24–25, 14476 Potsdam, Germany. Received: 17 November 2019; Accepted: 31 December 2019; Published: 3 January 2020 Abstract: We report on a novel RNA virus infecting the wasp Lysiphlebus fabarum, a parasitoid of aphids. This virus, tentatively named “Lysiphlebus fabarum virus” (LysV), was discovered in transcriptome sequences of wasps from an experimental evolution study in which the parasitoids were allowed to adapt to aphid hosts (Aphis fabae) with or without resistance-conferring endosymbionts. Based on phylogenetic analyses of the viral RNA-dependent RNA polymerase (RdRp), LysV belongs to the Iflaviridae family in the order of the Picornavirales, with the closest known relatives all being parasitoid wasp-infecting viruses. We developed an endpoint PCR and a more sensitive qPCR assay to screen for LysV in field samples and laboratory lines. These screens verified the occurrence of LysV in wild parasitoids and identified the likely wild-source population for lab infections in Western Switzerland. Three viral haplotypes could be distinguished in wild populations, of which two were found in the laboratory. -
Eesha Acharya Project #1
Eesha Acharya Project #1 Completed Project, Science, Health and Medical Measuring Vitamin C Levels in Cooked Foods Most people know that raw foods contain the most nutrients. However, many people prefer eating cooked foods. the problem is vitamin C is a water-soluble vitamin, so when foods are cooked they lose a lot of this essential nutrient. The purpose of this research is to determine which cooking method best retains the most vitamin C in vegetables. The raw vegetable vitamin C information will be compared to that of other cooking methods (grilling, boiling, and steaming) of that same vegetable. tomatoes, brussel sprouts, kale, bell peppers, broccoli, peas, and a tincture of iodine solution, 2-7% elemental iodine, will be used to test the vitamin C content. The food will be tested by mixing 10g of food to a starch-water mixture and straining the water. Drops of iodine will be added to the strained water until the solution turns black. The more iodine added, means the more vitamin C is in the food. Then the number of drops will be divided by 10g of food. This gives the drops per gram of food. This number will be multiplied by the factor. The drops per gram multiplied by the factor equals mg of vitamin C per gram of food This study is designed to help people consume more vitamin C. Many people in the United States have a vitamin C deficiency. Vitamin C is a key that prevents immune system deficiency and cardiovascular disease. So if a proper cooking method can be found, then people can consume more Vitamin C. -
Journal of Virology
JOURNAL OF VIROLOGY Volume 68 November 1994 No. 11 MINIREVIEW Molecular Biology of the Human Immunodeficiency Virus Ramu A. Subbramanian and Eric 6831-6835 Accessory Proteins A. Cohen ANIMAL VIRUSES Monoclonal Antibodies against Influenza Virus PB2 and NP J. Baircena, M. Ochoa, S. de la 6900-6909 Polypeptides Interfere with the Initiation Step of Viral Luna, J. A. Melero, A. Nieto, J. mRNA Synthesis In Vitro Ortin, and A. Portela Low-Affinity E2-Binding Site Mediates Downmodulation of Frank Stubenrauch and Herbert 6959-6966 E2 Transactivation of the Human Papillomavirus Type 8 Pfister Late Promoter Template-Dependent, In Vitro Replication of Rotavirus RNA Dayue Chen, Carl Q.-Y. Zeng, 7030-7039 Melissa J. Wentz, Mario Gorziglia, Mary K. Estes, and Robert F. Ramig Improved Self-Inactivating Retroviral Vectors Derived from Paul Olson, Susan Nelson, and 7060-7066 Spleen Necrosis Virus Ralph Dornburg Isolation of a New Foamy Retrovirus from Orangutans Myra 0. McClure, Paul D. 7124-7130 Bieniasz, Thomas F. Schulz, Ian L. Chrystie, Guy Simpson, Adriano Aguzzi, Julian G. Hoad, Andrew Cunningham, James Kirkwood, and Robin A. Weiss Cell Lines Inducibly Expressing the Adeno-Associated Virus Christina Holscher, Markus Horer, 7169-7177 (AAV) rep Gene: Requirements for Productive Replication Jurgen A. Kleinschmidt, of rep-Negative AAV Mutants Hanswalter Zentgraf, Alexander Burkle, and Regine Heilbronn Role of Flanking E Box Motifs in Human Immunodeficiency S.-H. Ignatius Ou, Leon F. 7188-7199 Virus Type 1 TATA Element Function Garcia-Martinez, Eyvind J. Paulssen, and Richard B. Gaynor Characterization and Molecular Basis of Heterogeneity of Fernando Rodriguez, Carlos 7244-7252 the African Swine Fever Virus Envelope Protein p54 Alcaraz, Adolfo Eiras, Rafael J. -
Downloads/ Hsp90interactors.Pdf), and Tend to Be Metastable, Being Rapidly Degraded Upon Hsp90 Inhibition
viruses Review Chaperoning the Mononegavirales: Current Knowledge and Future Directions Victor Latorre †, Florian Mattenberger † and Ron Geller * Institute for Integrative Systems Biology (I2SysBio), Universitat de Valencia-CSIC, 46980 Valencia, Spain; [email protected] (V.L.); [email protected] (F.M.) * Correspondence: [email protected]; Tel.: +34-963-543-187 † These authors contributed equally to this work. Received: 16 November 2018; Accepted: 5 December 2018; Published: 8 December 2018 Abstract: The order Mononegavirales harbors numerous viruses of significant relevance to human health, including both established and emerging infections. Currently, vaccines are only available for a small subset of these viruses, and antiviral therapies remain limited. Being obligate cellular parasites, viruses must utilize the cellular machinery for their replication and spread. Therefore, targeting cellular pathways used by viruses can provide novel therapeutic approaches. One of the key challenges confronted by both hosts and viruses alike is the successful folding and maturation of proteins. In cells, this task is faced by cellular molecular chaperones, a group of conserved and abundant proteins that oversee protein folding and help maintain protein homeostasis. In this review, we summarize the current knowledge of how the Mononegavirales interact with cellular chaperones, highlight key gaps in our knowledge, and discuss the potential of chaperone inhibitors as antivirals. Keywords: Mononegavirales; chaperones; antivirals; Hsp70; -
Structure of the Cleavage-Activated Prefusion Form of the Parainfluenza Virus 5 Fusion Protein
Structure of the cleavage-activated prefusion form of the parainfluenza virus 5 fusion protein Brett D. Welcha,b,1, Yuanyuan Liua,b,1, Christopher A. Korsa,b, George P. Lesera,b, Theodore S. Jardetzkyc,2, and Robert A. Lamba,b,2 aHoward Hughes Medical Institute and bDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208; and cDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305 Contributed by Robert A. Lamb, August 9, 2012 (sent for review June 28, 2012) The paramyxovirus parainfluenza virus 5 (PIV5) enters cells by refolding, resulting in formation of a trimeric coiled coil com- fusion of the viral envelope with the plasma membrane through posed of a heptad repeat A region that extends away from the the concerted action of the fusion (F) protein and the receptor viral membrane (18–20). binding protein hemagglutinin-neuraminidase. The F protein folds Peptide inhibitor studies and available atomic structures in- initially to form a trimeric metastable prefusion form that is trig- dicate that many of the key elements of this entry mechanism are gered to undergo large-scale irreversible conformational changes common to other class I viral fusion proteins, such as the hem- to form the trimeric postfusion conformation. It is thought that agglutinin (HA) of influenza virus, gp120/41 of HIV, S protein of F refolding couples the energy released with membrane fusion. severe acute respiratory syndrome coronavirus, and glycoprotein The F protein is synthesized as a precursor (F0) that must be (GP) of Ebola virus (reviewed in ref. 4). Although X-ray struc- cleaved by a host protease to form a biologically active molecule, tures of the six-helix bundle of many type I fusion proteins have F1,F2. -
Gifc-2018 Book of Abstracts
GIFC-2018 Giornate Italo-Francesi di Chimica Journées Franco-Italiennes de Chimie 16 – 18 April 2018 Grand Hotel Savoia Via Arsenale di Terra, 5 Genova BOOK OF ABSTRACTS ISBN: 978-88-94952-00-1 Gold Sponsors Silver Sponsors Patronages 2 3 Scientific Program 4 5 6 List of Posters (according to alphabetic order of presenting Authors) 1st session, Monday 16th April Num Cognome Nome Contatto Titolo Synthesis, purification and characterization of PO1 Aboudou Soioulata [email protected] antimicrobial peptides isolated from animal venoms [email protected] PO2 Ajmalghan Muthali Coverage dependent recombination mechanisms of hydrogen from niv-amu.fr tungsten surfaces via density functional theory Hybrid squaraine-silica nanoparticles as nir probes for biological PO3 Alberto Gabriele [email protected] applications: optimization of the photoemission performances Synthesis of doped metal oxide nanocrystals for solution-processed PO4 Alkarsifi Riva [email protected] interfacial layers in organic solar cells PO5 Anceschi Anastasia [email protected] Maltodextrins nanosponges as precursor for porous carbon materials [email protected] PO7 Arnodo Davide First racemic total synthesis of heliolactone .it [email protected]. PO8 Azzi Emanuele Synthesis of boronated analogue of curcumin as potential therapeutical it agents for alzheimer’s disease Study of Nanobiomaterials with Bio-based Antioxidants: Interaction of PO9 Barzan Giulia Sci piem Polyphenol Molecules with Hydroxyapatite and Silica Luigi Methotrexate loaded solid lipid nanoparticles: protein functionalization to PO10 Battaglia [email protected] Sebastiano improve brain biodistribution [email protected] PO11 Begni Federico On the adsorption of toluene on porous materials with different chemical m composition Synthesischaracterization of activated carbon from modified banana peels PO12 Ben Khalifa Eya [email protected] for hexavalent chromium adsorption [email protected] PO13 Benvenuti Martino The maturation of the co-dehydrogenase from thermococcus sp.