Inhibition of HIV-1 by an Anti-Integrase Single-Chain Variable
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Oncogenes of DNA Tumor Viruses1
[CANCER RESEARCH 48. 493-496. February I. 1988] Perspectives in Cancer Research Oncogenes of DNA Tumor Viruses1 Arnold J. Levine Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544 Experiments carried out over the past 10-12 years have the cellular oncogenes. It will attempt to identify where more created a field or approach which may properly be termed the information is required or contradictions appear in the devel molecular basis of cancer. One of its major accomplishments oping concepts. Finally, this communication will examine ex has been the identification and understanding of some of the amples of cooperation between oncogenes and other gene prod functions of a group of cancer-causing genes, the oncogenes. ucts which modify the mode of action of the former. If we are The major path to the oncogenes came from the study of cancer- on the right track, then general principles may well emerge. causing viruses. The oncogenes have been recognized and stud Tumor formation in animals or transformation in cell culture ied by two separate but related groups of virologists focusing has been demonstrated with many different DNA-containing upon either the DNA (1) or RNA (2) tumor viruses (they even viruses (1). In most cases it has been possible to identify one or have separate meetings now that these fields have grown so a few viral genes and their products that are responsible for large). From their studies it has become clear that the oncogenes transformation or, in some cases, tumorigenesis. A list of these of each virus type have very different origins. -
Tätigkeitsbericht 2007/2008
Tätigkeitsbericht 2007/2008 8 200 / 7 0 20 Tätigkeitsbericht Stiftung bürgerlichen Rechts Martinistraße 52 · 20251 Hamburg Tel.: +49 (0) 40 480 51-0 · Fax: +49 (0) 40 480 51-103 [email protected] · www.hpi-hamburg.de Impressum Verantwortlich Prof. Dr. Thomas Dobner für den Inhalt Dr. Heinrich Hohenberg Redaktion Dr. Angela Homfeld Dr. Nicole Nolting Grafik & Layout AlsterWerk MedienService GmbH Hamburg Druck Hartung Druck + Medien GmbH Hamburg Titelbild Neu gestaltete Fassade des Seuchenlaborgebäudes Tätigkeitsbericht 2007/2008 Heinrich-Pette-Institut für Experimentelle Virologie und Immunologie an der Universität Hamburg Martinistraße 52 · 20251 Hamburg Postfach 201652 · 20206 Hamburg Telefon: +49-40/4 80 51-0 Telefax: +49-40/4 80 51-103 E-Mail: [email protected] Internet: www.hpi-hamburg.de Das Heinrich-Pette-Institut ist Mitglied der Leibniz-Gemeinschaft (WGL) Internet: www.wgl.de Inhaltsverzeichnis Allgemeiner Überblick Vorwort ................................................................................................... 1 Die Struktur des Heinrich-Pette-Instituts .............................................. 2 Modernisierung des HPI erfolgreich abgeschlossen ............................ 4 60 Jahre HPI .............................................................................................. 5 Offen für den Dialog .............................................................................. 6 Preisverleihungen und Ehrungen .......................................................... 8 Personelle Veränderungen in -
Evolution of Hepatitis B Serological Markers in HIV Coinfected Patients: a Case Study
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Cadernos Espinosanos (E-Journal) Rev Saúde Pública 2017;51:24 Artigo Original http://www.rsp.fsp.usp.br/ Evolution of hepatitis B serological markers in HIV coinfected patients: a case study Ana Luiza de Castro Conde ToscanoI,II, Maria Cássia Mendes CorrêaII,III I Instituto de Infectologia Emílio Ribas. São Paulo, SP, Brasil II Departamento de Doenças Infecciosas. Faculdade de Medicina. Universidade de São Paulo. São Paulo, SP, Brasil III Instituto de Medicina Tropical de São Paulo. Laboratório de Investigação Médica 52. São Paulo, SP, Brasil ABSTRACT OBJECTIVE: To describe the evolution of serological markers among HIV and hepatitis B coinfected patients, with emphasis on evaluating the reactivation or seroreversion of these markers. METHODS: The study population consisted of patients met in an AIDS Outpatient Clinic in São Paulo State, Brazil. We included in the analysis all HIV-infected and who underwent at least two positive hepatitis B surface antigen serological testing during clinical follow up, with tests taken six months apart. Patients were tested with commercial kits available for hepatitis B serological markers by microparticle enzyme immunoassay. Clinical variables were collected: age, sex, CD4+ T-cell count, HIV viral load, alanine aminotransferase level, exposure to antiretroviral drugs including lamivudine and/or tenofovir. RESULTS: Among 2,242 HIV positive patients, we identified 105 (4.7%) patients with chronic hepatitis B. Follow up time for these patients varied from six months to 20.5 years. All patients underwent antiretroviral therapy during follow-up. Among patients with chronic hepatitis B, 58% were hepatitis B “e” antigen positive at the first assessment. -
Covalent Protein Display on Hepatitis B Core-Like Particles in Plants
www.nature.com/scientificreports OPEN Covalent protein display on Hepatitis B core‑like particles in plants through the in vivo use of the SpyTag/SpyCatcher system Hadrien Peyret1*, Daniel Ponndorf1, Yulia Meshcheriakova1, Jake Richardson2 & George P. Lomonossof1 Virus‑like particles (VLPs) can be used as nano‑carriers and antigen‑display systems in vaccine development and therapeutic applications. Conjugation of peptides or whole proteins to VLPs can be achieved using diferent methods such as the SpyTag/SpyCatcher system. Here we investigate the conjugation of tandem Hepatitis B core (tHBcAg) VLPs and the model antigen GFP in vivo in Nicotiana benthamiana. We show that tHBcAg VLPs could be successfully conjugated with GFP in the cytosol and ER without altering VLP formation or GFP fuorescence. Conjugation in the cytosol was more efcient when SpyCatcher was displayed on tHBcAg VLPs instead of being fused to GFP. This efect was even more obvious in the ER, showing that it is optimal to display SpyCatcher on the tHBcAg VLPs and SpyTag on the binding partner. To test transferability of the GFP results to other antigens, we successfully conjugated tHBcAg VLPs to the HIV capsid protein P24 in the cytosol. This work presents an efcient strategy which can lead to time and cost saving post‑translational, covalent conjugation of recombinant proteins in plants. Virus-like particles (VLPs) are protein complexes that are similar or even indistinguishable from native viral particles in terms of their structure and antigenicity. Tey do not contain the viral genome and hence, they cannot replicate and are not pathogenic. Te repetitive surface structure and a typical size range of 20–200 nm make VLPs highly immunogenic and they can induce a strong humoral and cellular immune response1. -
A Rapid Immunochromatographic Method Based on a Secondary Antibody-Labelled Magnetic Nanoprobe for the Detection of Hepatitis B Pres2 Surface Antigen
biosensors Article A Rapid Immunochromatographic Method Based on a Secondary Antibody-Labelled Magnetic Nanoprobe for the Detection of Hepatitis B preS2 Surface Antigen Yangyang Cai 1,2,3, Jun Yan 1,2,3, Li Zhu 4, Hengliang Wang 4 and Ying Lu 1,2,3,* 1 College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China; [email protected] (Y.C.); [email protected] (J.Y.) 2 Laboratory of Quality & Safety Risk Assessment for Aquatic Products on Storage and Preservation (Shanghai), Ministry of Agriculture, Shanghai 201306, China 3 Shanghai Engineering Research Center of Aquatic-Product Processing and Preservation, Shanghai 201306, China 4 Beijing Institute of Biotechnology, Beijing 100071, China; [email protected] (L.Z.); [email protected] (H.W.) * Correspondence: [email protected]; Tel.: +86-021-6190-0503 Received: 24 September 2020; Accepted: 27 October 2020; Published: 31 October 2020 Abstract: Hepatitis B is a globally prevalent viral infectious disease caused by the hepatitis B virus (HBV). In this study, an immunochromatographic assay (ICA) for the rapid detection of hepatitis B preS2 antigen (preS2Ag) was established. The magnetic nanoparticles (MNPs) indirectly labelled with goat anti-mouse (GAM) secondary antibody were applied as a nanoprobe for free preS2 antibody (preS2Ab) capturing and signal amplification. By employing sample pre-incubation processing as well, preS2Ag-preS2Ab was sufficiently caught by the GAM-MNPs probe in 5 min. A qualitative sensitivity of 625 ng/mL was obtained by naked-eye observation within 15–20 min. A standard curve (0–5000 ng/mL) was established, with a quantitative limit of detection (LOD) of 3.6 ng/mL, based on the stability and penetrability of the magnetic signal characteristics. -
Hepatitis B Virus X Protein Inhibits P53 Sequence-Specific DNA Binding
Proc. Nati. Acad. Sci. USA Vol. 91, pp. 2230-2234, March 1994 Medical Sciences Hepatitis B virus X protein inhibits p53 sequence-specific DNA binding, transcriptional activity, and association with transcription factor ERCC3 XIN WEI WANG*, KATHLEEN FORRESTER*, HEIDI YEH*, MARK A. FEITELSONt, JEN-REN GUI, AND CURTIS C. HARRIS*§ *Laboratory of Human Carcinogenesis, Division of Cancer Etiology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892; tDepartment of Pathology and Cell Biology, Jefferson Medical College, Philadelphia, PA 19107; and tDepartment of Molecular Biology and Biochemistry, Shanghai Cancer Institute, Shanghai, People's Republic of China. Communicated by Bert Vogelstein, December 27, 1993 (receivedfor review December 9, 1993) ABSTRACT Chronic active hepatitis caused by infection about the role of HBX in HCC development. In this report, with hepatitis B virus, a DNA virus, is a major risk factor for we present results consistent with the hypothesis that HBX human hepatocellular carcinoma. Since the oncogenicity of binds to p53 and abrogates its normal cellular functions. several DNA viruses is dependent on the interaction of their viral oncoproteins with cellular tumor-suppressor gene prod- MATERIAL AND METHODS ucts, we investigated the interaction between hepatitis B virus X protein (HBX) and human wild-type p53 protein. HBX Plasmids. Plasmid constructs encoding GST-p53-WT, con- complexes with the wild-type p53 protein and inhibits its taining glutathione S-transferase (GST) fused to human wild- sequence-specific DNA binding in vitro. HBX expresslin also type p53, and GST-p53-135Y, containing GST fused to the inhibits p53-mediated transcrptional activation in vivo and the mutant p53 containing a His -* Tyr mutation at codon 135, in vitro asoition of p53 and ERCC3, a general transcription were provided by Jon Huibregtse (National Cancer Institute) factor involved in nucleotide excision repair. -
PP2A-Dependent Disruption of Centrosome Replication and Cytoskeleton Organization in Drosophila by SV40 Small Tumor Antigen
Oncogene (2008) 27, 6334–6346 & 2008 Macmillan Publishers Limited All rights reserved 0950-9232/08 $32.00 www.nature.com/onc ORIGINAL ARTICLE PP2A-dependent disruption of centrosome replication and cytoskeleton organization in Drosophila by SV40 small tumor antigen S Kotadia1,LRKao1, SA Comerford2, RT Jones1, RE Hammer3 and TL Megraw1 1Department of Pharmacology, The Cecil and Ida Green Center for Reproductive Biology Sciences, The University of Texas Southwestern Medical Center at Dallas, Dallas, TX, USA; 2Department of Molecular Genetics, The Cecil and Ida Green Center for Reproductive Biology Sciences, The University of Texas Southwestern Medical Center at Dallas, Dallas, TX, USA and 3Department of Biochemistry, The Cecil and Ida Green Center for Reproductive Biology Sciences, The University of Texas Southwestern Medical Center at Dallas, Dallas, TX, USA Viruses of the DNA tumor virus family share the ability to cell-cycle and apoptosis regulation, viral oncoproteins transform vertebrate cells through the action of virus- transform cells. Investigation of DNA tumor virus encoded tumor antigens that interfere with normal cell oncoproteins has led to the identification of many physiology. They accomplish this very efficiently by fundamental mechanisms of tumor suppression (Lavia inhibiting endogenous tumor suppressor proteins that et al., 2003; Ahuja et al., 2005). By altering the activity control cell proliferation and apoptosis. Simian virus 40 of p53, retinoblastoma protein and serine/threonine (SV40) encodes two oncoproteins, large tumor antigen, protein phosphatase 2A (PP2A), three key tumor which directly inhibits the tumor suppressors p53 and Rb, suppressors, SV40 can cause tumor formation in and small tumor antigen (ST), which interferes with transgenic mouse models (Ahuja et al., 2005; Arroyo serine/threonine protein phosphatase 2A (PP2A). -
The Simian Virus 40 Large Tumor Antigen Activates Csrc and Requires Csrc for Full Neoplastic Transformation
ANTICANCER RESEARCH 30: 47-54 (2010) The Simian Virus 40 Large Tumor Antigen Activates cSrc and Requires cSrc for Full Neoplastic Transformation ROZANNE ARULANANDAM, MULU GELETU and LEDA RAPTIS Departments of Microbiology and Immunology and Pathology, Queen's University, Kingston, Ontario, K7L 3N6, Canada Abstract. Aim: To investigate the role of the cellular The effects of TAg on the Rb family proteins are thought to be protooncogene product, cSrc, in neoplastic transformation by exerted by regulating the activity of the E2F transcription factors. the large tumor antigen of simian virus 40 (TAg), the ability of There are eight known E2F proteins (E2F1-8), all of which TAg to increase cSrc activity was examined. Materials and possess a DNA-binding domain that governs their interactions Methods: cSrc activity was measured in cells expressing wild- with a common consensus sequence present in the promoters of type or mutant TAg and compared to the parental line. Results: a number of genes (reviewed in (4, 5)). In quiescent cells, E2F- The results indicated that TAg expression in mouse 3T3 regulated genes are not expressed because their promoters are fibroblasts causes a dramatic increase in cSrc activity, a finding occupied primarily by p130/E2F4 complexes which repress which establishes TAg as a cSrc activator. This ability transcription. Following receptor stimulation, Rb proteins are depended upon a TAg, intact retinoblastoma-susceptibility gene inactivated through phosphorylation by the cyclin-dependent product (Rb) family-binding site. In addition, genetic ablation kinases and this results in the replacement of the p130/E2F4 of pRb in mouse fibroblasts increased cSrc activity, suggesting complexes by the ‘activating’ E2F1-3. -
Laboratory Testing
Laboratory Testing Laboratory Testing for Initial Assessment and Monitoring of Patients with HIV Receiving Antiretroviral Therapy (Last updated December 18, 2019; last reviewed December 18, 2019) Several laboratory tests are important for initial evaluation of people with HIV upon entry into care, and some tests should be performed before and after initiation or modification of antiretroviral therapy (ART) to assess the virologic and immunologic efficacy of ART and to monitor for laboratory abnormalities that may be associated with antiretroviral (ARV) drugs. Table 3 outlines recommendations on the frequency of testing from the Panel on Antiretroviral Guidelines for Adults and Adolescents. As noted in the table, some tests may be repeated more frequently if clinically indicated. Two surrogate markers are used to monitor people with HIV: plasma HIV RNA (viral load) to assess level of HIV viremia and CD4 T lymphocyte cell count to assess immune function. Standard (reverse transcriptase and protease) genotypic resistance testing should be used to guide selection of an ARV regimen; if transmitted integrase strand transfer inhibitor resistance is a concern, testing should also include the integrase gene (see Drug-Resistance Testing). For guidance on ART regimens to use when resistance testing results are unavailable, clinicians should consult What to Start. A viral tropism assay should be performed before initiation of a CCR5 antagonist or at the time of virologic failure that occurs while a patient is receiving a CCR5 antagonist. HLA-B*5701 testing should be performed before initiation of abacavir (ABC). Patients should be screened for hepatitis B and hepatitis C virus infection before initiating ART and, if indicated, periodically after ART initiation, as treatment of these coinfections may affect the choice of ART and likelihood of drug-induced hepatotoxicity. -
Complementation of Recombinant Baculoviruses by Coinfection With
Proc. Natl. Acad. Sci. USA Vol. 86, pp. 1453-1456, March 1989 Biochemistry Complementation of recombinant baculoviruses by coinfection with wild-type virus facilitates production in insect larvae of antigenic proteins of hepatitis B virus and influenza virus (baculovirus/hepatitis B surface antigen/influenza A virus neuraminidase) PETER M. PRICE*, CHARLES F. REICHELDERFERt, BERT E. JOHANSSON*, EDWIN D. KILBOURNE, AND GEORGE ACS*§ Departments of *Biochemistry, tMicrobiology, and §Neoplastic Diseases, Mount Sinai School of Medicine of the City University of New York, New York, NY 10029; and tDepartment of Entomology, University of Maryland, College Park, MD 20742 Contributed by Edwin D. Kilbourne, November 21, 1988 ABSTRACT We describe the coinfection of insects with In the present paper, we describe a strategy to increase the wild-type and recombinant baculoviruses in which the polyhe- in vivo infection rate of recombinant viruses and we demon- drin gene promoter is used to express hepatitis B virus envelope strate its efficiency in producing high yields of two foreign protein (hepatitis B virus surface antigen; HBsAg) or influenza viral proteins, hepatitis B virus (HBV) surface antigen (HBs- A virus neuraminidase (NA). Viruses were administeredper os Ag) and influenza A virus neuraminidase (NA). This strata- to larvae of the cabbage looper, Trichoplusia ni, causing an gem involves complementation through dual infection of infection that within 5 days resulted in the production of -O.15 recombinant and wild-type baculoviruses to produce encap- mg of HBsAg per insect, representing 1.5% of the total sidated recombinant virus particles that readily infect Tri- extracted protein, or =2.8 mg of NA per insect, representing choplusia ni larvae when given by the oral route. -
Identification of Rab18 As an Essential Host Factor for Bkpyv Infection Using a Whole Genome RNA 2 Interference Screen
bioRxiv preprint doi: https://doi.org/10.1101/157602; this version posted June 29, 2017. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. 1 Identification of Rab18 as an Essential Host Factor for BKPyV Infection Using a Whole Genome RNA 2 Interference Screen 3 4 Linbo Zhaoa, Michael J. Imperialea,b,* 5 6 aDepartment of Microbiology and Immunology, bComprehensive Cancer Center, University of Michigan, 7 Ann Arbor, MI, 48109, USA 8 9 10 11 12 13 14 15 16 17 18 * Corresponding author. Department of Microbiology and Immunology, 1150 West Medical Center 19 Drive, 5724 Medical Science II, Ann Arbor, MI 48109-5620, USA. Tel. +1 (734) 763 9162. Fax: +1 (734) 20 764 3562. 21 E-mail addresses: [email protected] (L. Zhao); [email protected] (M.J. Imperiale). 22 23 24 1 bioRxiv preprint doi: https://doi.org/10.1101/157602; this version posted June 29, 2017. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. 25 Abstract 26 27 BK polyomavirus (BKPyV) is a human pathogen first isolated in 1971. BKPyV infection is ubiquitous in the 28 human population, with over 80% of adults worldwide being seropositive for BKPyV. BKPyV infection is 29 usually asymptomatic; however, BKPyV reactivation in immunosuppressed transplant patients causes 30 two diseases, polyomavirus-associated nephropathy and hemorrhagic cystitis. -
ABBOTT PRISM HIV O Plus 3L68-68 G10316R06 Read Highlighted Changes: Human Immunodeficiency Virus Revised March 2019 Types 1 and 2 (E
en ABBOTT PRISM HIV O Plus 3L68-68 G10316R06 Read Highlighted Changes: Human Immunodeficiency Virus Revised March 2019 Types 1 and 2 (E. coli, B. megaterium, Recombinant) Antigen and Synthetic Peptide Customer Service: Contact your local representative or find country specific contact information on www.abbottdiagnostics.com Package insert instructions must be carefully followed. Reliability of assay results cannot be guaranteed if there are any deviations from the instructions in this package insert. Key to Symbols Caution Conjugate Wash PROBE 20X CONC Probe 20X Concentrate Contains Sodium Azide. Consult instructions Contact with acids liberates PROBE DILUENT Probe Diuent for use very toxic gas. Manufacturer Danger: Reproductive Hazard Probe Wash Store at 2-8°C Distributed by Produced for Abbott by Authorized Representative in Store at 15-30°C Product of USA the European Community Use by/Expiration HIV-1 CONTROL + HIV-1 Positive Control Purge Concentrate date Activator HIV-2 CONTROL + HIV-2 Positive Control Reaction Trays Concentrate In Vitro Diagnostic Medical Activator Diluent Reagent Components Device Activator Line Line Cleaner List Number Treatment Assay Kit Card Lot Number Run Control Adapters Negative Calibrator Master Lot Sample Cups Positive Calibrator Microparticles Transfer Wash Warning: May cause an Calibrators Pipette Tips allergic reaction Conjugate Prime/Purge Accessories Warning: Severe Irritant See REAGENTS section for a full explanation of symbols used in reagent component naming. U.S. License No. 43 1 NAME AND INTENDED USE The amount of light emitted is proportional to the amount of anti-HIV-1 The ABBOTT PRISM HIV O Plus assay is an in vitro chemiluminescent and/or anti-HIV-2 in the sample.