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Viral glycoprotein-D

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https://www.readbyqxmd.com/read/27909702/complement-inhibition-enables-tumor-delivery-of-lcmv-glycoprotein-pseudotyped-viruses-in-the-presence-of-antiviral-antibodies
#1
Laura Evgin, Carolina S Ilkow, Marie-Claude Bourgeois-Daigneault, Christiano Tanese de Souza, Lawton Stubbert, Michael S Huh, Victoria A Jennings, Monique Marguerie, Sergio A Acuna, Brian A Keller, Charles Lefebvre, Theresa Falls, Fabrice Le Boeuf, Rebecca A Auer, John D Lambris, J Andrea McCart, David F Stojdl, John C Bell
The systemic delivery of therapeutic viruses, such as oncolytic viruses or vaccines, is limited by the generation of neutralizing antibodies. While pseudotyping of rhabdoviruses with the lymphocytic choriomeningitis virus glycoprotein has previously allowed for multiple rounds of delivery in mice, this strategy has not translated to other animal models. For the first time, we provide experimental evidence that antibodies generated against the lymphocytic choriomeningitis virus glycoprotein mediate robust complement-dependent viral neutralization via activation of the classical pathway...
2016: Molecular Therapy Oncolytics
https://www.readbyqxmd.com/read/27868164/efficient-production-of-recombinant-glycoprotein-d-of-herpes-simplex-virus-type-2-in-pichia-pastoris-and-its-protective-efficacy-against-viral-challenge-in-mice
#2
Man Wang, Shuai Jiang, Li Zhou, Chaoqun Wang, Ruifeng Mao, Murugavel Ponnusamy
Herpes simplex virus type 2 (HSV-2) infection is the leading cause of genital ulcer disease and a significant public health concern. However, there are no approved vaccines available to prevent HSV-2 infection. The glycoprotein D (gD) of HSV-2 is the most important candidate antigen for vaccine development. In this study, a truncated form of gD (codons 1-340, gD1-340) was produced as a secretory protein in the methylotrophic yeast Pichia pastoris. The recombinant gD1-340 with a His6 tag was purified to homogeneity by one-step affinity chromatography...
November 21, 2016: Archives of Virology
https://www.readbyqxmd.com/read/27814506/ebola-virus-glycoprotein-with-increased-infectivity-dominated-the-2013-2016-epidemic
#3
William E Diehl, Aaron E Lin, Nathan D Grubaugh, Luiz Max Carvalho, Kyusik Kim, Pyae Phyo Kyawe, Sean M McCauley, Elisa Donnard, Alper Kucukural, Patrick McDonel, Stephen F Schaffner, Manuel Garber, Andrew Rambaut, Kristian G Andersen, Pardis C Sabeti, Jeremy Luban
The magnitude of the 2013-2016 Ebola virus disease (EVD) epidemic enabled an unprecedented number of viral mutations to occur over successive human-to-human transmission events, increasing the probability that adaptation to the human host occurred during the outbreak. We investigated one nonsynonymous mutation, Ebola virus (EBOV) glycoprotein (GP) mutant A82V, for its effect on viral infectivity. This mutation, located at the NPC1-binding site on EBOV GP, occurred early in the 2013-2016 outbreak and rose to high frequency...
November 3, 2016: Cell
https://www.readbyqxmd.com/read/27789948/hepatitis-c-virus-e2-protein-encapsulation-into-poly-d-l-lactic-co-glycolide-microspheres-could-induce-mice-cytotoxic-t-cell-response
#4
Piyachat Roopngam, Kewei Liu, Lin Mei, Yi Zheng, Xianbing Zhu, Hsiang-I Tsai, Laiqiang Huang
Hepatitis C virus (HCV) is known to cause hepatitis and hepatocellular carcinoma. E2 envelope glycoprotein of HCV type (HCV-E2) has been reported to bind human host cells and is a major target for developing anti-HCV vaccines. However, the therapeutic vaccine for infected patients still needs further development. The vaccine aims to provide cytotoxic T-cells to eliminate infected cells and hepatocellular carcinoma. Currently, there is no effective HCV therapeutic vaccine because most chronically infected patients rarely generate cytotoxic T-cells, even though they have high levels of neutralizing antibodies...
2016: International Journal of Nanomedicine
https://www.readbyqxmd.com/read/27783711/mechanistic-insight-into-bunyavirus-induced-membrane-fusion-from-structure-function-analyses-of-the-hantavirus-envelope-glycoprotein-gc
#5
Pablo Guardado-Calvo, Eduardo A Bignon, Eva Stettner, Scott Allen Jeffers, Jimena Pérez-Vargas, Gerard Pehau-Arnaudet, M Alejandra Tortorici, Jean-Luc Jestin, Patrick England, Nicole D Tischler, Félix A Rey
Hantaviruses are zoonotic viruses transmitted to humans by persistently infected rodents, giving rise to serious outbreaks of hemorrhagic fever with renal syndrome (HFRS) or of hantavirus pulmonary syndrome (HPS), depending on the virus, which are associated with high case fatality rates. There is only limited knowledge about the organization of the viral particles and in particular, about the hantavirus membrane fusion glycoprotein Gc, the function of which is essential for virus entry. We describe here the X-ray structures of Gc from Hantaan virus, the type species hantavirus and responsible for HFRS, both in its neutral pH, monomeric pre-fusion conformation, and in its acidic pH, trimeric post-fusion form...
October 2016: PLoS Pathogens
https://www.readbyqxmd.com/read/27783673/crystal-structure-of-glycoprotein-c-from-a-hantavirus-in-the-post-fusion-conformation
#6
Shmuel Willensky, Hagit Bar-Rogovsky, Eduardo A Bignon, Nicole D Tischler, Yorgo Modis, Moshe Dessau
Hantaviruses are important emerging human pathogens and are the causative agents of serious diseases in humans with high mortality rates. Like other members in the Bunyaviridae family their M segment encodes two glycoproteins, GN and GC, which are responsible for the early events of infection. Hantaviruses deliver their tripartite genome into the cytoplasm by fusion of the viral and endosomal membranes in response to the reduced pH of the endosome. Unlike phleboviruses (e.g. Rift valley fever virus), that have an icosahedral glycoprotein envelope, hantaviruses display a pleomorphic virion morphology as GN and GC assemble into spikes with apparent four-fold symmetry organized in a grid-like pattern on the viral membrane...
October 2016: PLoS Pathogens
https://www.readbyqxmd.com/read/27764150/stability-characterization-of-a-vaccine-antigen-based-on-the-respiratory-syncytial-virus-fusion-glycoprotein
#7
Jessica A Flynn, Eberhard Durr, Ryan Swoyer, Pedro J Cejas, Melanie S Horton, Jennifer D Galli, Scott A Cosmi, Amy S Espeseth, Andrew J Bett, Lan Zhang
Infection with Respiratory Syncytial Virus (RSV) causes both upper and lower respiratory tract disease in humans, leading to significant morbidity and mortality in both young children and older adults. Currently, there is no licensed vaccine available, and therapeutic options are limited. During the infection process, the type I viral fusion (F) glycoprotein on the surface of the RSV particle rearranges from a metastable prefusion conformation to a highly stable postfusion form. In people naturally infected with RSV, most potent neutralizing antibodies are directed to the prefusion form of the F protein...
2016: PloS One
https://www.readbyqxmd.com/read/27733647/in-vivo-efficacy-of-measles-virus-fusion-protein-derived-peptides-is-modulated-by-properties-of-self-assembly-and-membrane-residence
#8
T N Figueira, L M Palermo, A S Veiga, D Huey, C A Alabi, N C Santos, J C Welsch, C Mathieu, B Horvat, S Niewiesk, A Moscona, M A R B Castanho, M Porotto
: Measles virus (MV) infection is undergoing resurgence and remains one of the leading causes of death among young children worldwide despite the availability of an effective measles vaccine. MV infects its target cells by coordinated action of the MV hemagglutinin (H) and fusion (F) envelope glycoproteins; upon receptor engagement by H, the pre-fusion F undergoes a structural transition, extending and inserting into the target cell membrane and then re-folding into a post-fusion structure that fuses the viral and cell membranes...
October 12, 2016: Journal of Virology
https://www.readbyqxmd.com/read/27723487/herpes-simplex-virus-glycoprotein-d-relocates-nectin-1-from-intercellular-contacts
#9
Arjun K Bhargava, Paul W Rothlauf, Claude Krummenacher
Herpes simplex virus (HSV) uses the cell adhesion molecule nectin-1 as a receptor to enter neurons and epithelial cells. The viral glycoprotein D (gD) is used as a non-canonical ligand for nectin-1. The gD binding site on nectin-1 overlaps with a functional adhesive site involved in nectin-nectin homophilic trans-interaction. Consequently, when nectin-1 is engaged with a cellular ligand at cell junctions, the gD binding site is occupied. Here we report that HSV gD is able to disrupt intercellular homophilic trans-interaction of nectin-1 and induce a rapid redistribution of nectin-1 from cell junctions...
December 2016: Virology
https://www.readbyqxmd.com/read/27707922/syncytial-mutations-do-not-impair-the-specificity-of-entry-and-spread-of-a-glycoprotein-d-receptor-retargeted-herpes-simplex-virus
#10
Yu Okubo, Hiroaki Uchida, Aika Wakata, Takuma Suzuki, Tomoko Shibata, Hitomi Ikeda, Miki Yamaguchi, Justus B Cohen, Joseph C Glorioso, Mitsuo Tagaya, Hirofumi Hamada, Hideaki Tahara
: Membrane fusion, which is the key process for both initial cell entry and subsequent lateral spread of herpes simplex virus (HSV), requires the four envelope glycoproteins gB, gD, gH, and gL. Syncytial mutations, predominantly mapped to the gB and gK genes, confer hyperfusogenicity on HSV and cause multinucleated giant cells, termed syncytia. Here we asked whether interaction of gD with a cognate entry receptor remains indispensable for initiating membrane fusion of syncytial strains...
December 15, 2016: Journal of Virology
https://www.readbyqxmd.com/read/27641362/linear-biocompatible-glyco-polyamidoamines-as-dual-action-mode-virus-infection-inhibitors-with-potential-as-broad-spectrum-microbicides-for-sexually-transmitted-diseases
#11
Nicolò Mauro, Paolo Ferruti, Elisabetta Ranucci, Amedea Manfredi, Angela Berzi, Mario Clerici, Valeria Cagno, David Lembo, Alessandro Palmioli, Sara Sattin
The initial steps of viral infections are mediated by interactions between viral proteins and cellular receptors. Blocking the latter with high-affinity ligands may inhibit infection. DC-SIGN, a C-type lectin receptor expressed by immature dendritic cells and macrophages, mediates human immunodeficiency virus (HIV) infection by recognizing mannose clusters on the HIV-1 gp120 envelope glycoprotein. Mannosylated glycodendrimers act as HIV entry inhibitors thanks to their ability to block this receptor. Previously, an amphoteric, but prevailingly cationic polyamidoamine named AGMA1 proved effective as infection inhibitor for several heparan sulfate proteoglycan-dependent viruses, such as human papilloma virus HPV-16 and herpes simplex virus HSV-2...
2016: Scientific Reports
https://www.readbyqxmd.com/read/27640936/resistance-of-transmitted-founder-hiv-1-to-ifitm-mediated-restriction
#12
Toshana L Foster, Harry Wilson, Shilpa S Iyer, Karen Coss, Katie Doores, Sarah Smith, Paul Kellam, Andrés Finzi, Persephone Borrow, Beatrice H Hahn, Stuart J D Neil
Interferon-induced transmembrane proteins (IFITMs) restrict the entry of diverse enveloped viruses through incompletely understood mechanisms. While IFITMs are reported to inhibit HIV-1, their in vivo relevance is unclear. We show that IFITM sensitivity of HIV-1 strains is determined by the co-receptor usage of the viral envelope glycoproteins as well as IFITM subcellular localization within the target cell. Importantly, we find that transmitted founder HIV-1, which establishes de novo infections, is uniquely resistant to the antiviral activity of IFITMs...
October 12, 2016: Cell Host & Microbe
https://www.readbyqxmd.com/read/27635861/dendritic-cell-based-vaccines-in-treating-recurrent-herpes-labialis-results-of-pilot-clinical-study
#13
Olga Leplina, Nataliya Starostina, Olga Zheltova, Alexandr Ostanin, Ekaterina Shevela, Elena Chernykh
Recurrent herpes simplex labialis caused predominantly with herpes simplexvirus 1(HSV-1) is a major problem, for which various treatments have minimal impact. Given the important role of the immune system in controlling virus infection, an activation of virus-specific immune responses, in particular,using dendritic cell (DCs) vaccines, seems to be a promising approach for the treatment of patients with frequent recurrences of herpes labialis. The current paper presents the results of a pilot study of the safety and efficacy of DC vaccines in 14 patients with recurrent HSV-1 infections...
July 26, 2016: Human Vaccines & Immunotherapeutics
https://www.readbyqxmd.com/read/27605674/alteration-of-a-second-putative-fusion-peptide-of-structural-glycoprotein-e2-of-classical-swine-fever-virus-alters-virus-replication-and-virulence-in-swine
#14
L G Holinka, E Largo, D P Gladue, V O'Donnell, G R Risatti, J L Nieva, M V Borca
: E2, the major envelope glycoprotein of classical swine fever virus (CSFV), is involved in several critical virus functions, including cell attachment, host range susceptibility, and virulence in natural hosts. Functional structural analysis of E2 based on a Wimley-White interfacial hydrophobicity distribution predicted the involvement of a loop (residues 864 to 881) stabilized by a disulfide bond ((869)CKWGGNWTCV(878), named FPII) in establishing interactions with the host cell membrane...
November 15, 2016: Journal of Virology
https://www.readbyqxmd.com/read/27597813/development-of-a-liquid-chromatography-high-resolution-mass-spectrometry-method-for-the-quantitation-of-viral-envelope-glycoprotein-in-ebola-virus-like-particle-vaccine-preparations
#15
Lisa H Cazares, Michael D Ward, Ernst E Brueggemann, Tara Kenny, Paul Demond, Christopher R Mahone, Karen A O Martins, Jonathan E Nuss, Trevor Glaros, Sina Bavari
BACKGROUND: Ebola virus like particles (EBOV VLPs, eVLPs), are produced by expressing the viral transmembrane glycoprotein (GP) and structural matrix protein VP40 in mammalian cells. When expressed, these proteins self-assemble and bud from 'host' cells displaying morphology similar to infectious virions. Several studies have shown that rodents and non-human primates vaccinated with eVLPs are protected from lethal EBOV challenge. The mucin-like domain of envelope glycoprotein GP1 serves as the major target for a productive humoral immune response...
2016: Clinical Proteomics
https://www.readbyqxmd.com/read/27596163/differences-in-glyca-and-lipoprotein-particle-parameters-may-help-distinguish-acute-kawasaki-disease-from-other-febrile-illnesses-in-children
#16
Margery A Connelly, Chisato Shimizu, Deborah A Winegar, Irina Shalaurova, Ray Pourfarzib, James D Otvos, John T Kanegaye, Adriana H Tremoulet, Jane C Burns
BACKGROUND: Glycosylation patterns of serum proteins, such as α1-acid glycoprotein, are modified during an acute phase reaction. The response of acute Kawasaki disease (KD) patients to IVIG treatment has been linked to sialic acid levels on native IgG, suggesting that protein glycosylation patterns vary during the immune response in acute KD. Additionally, the distribution and function of lipoprotein particles are altered during inflammation. Therefore, the aim of this study was to explore the potential for GlycA, a marker of protein glycosylation, and the lipoprotein particle profile to distinguish pediatric patients with acute KD from those with other febrile illnesses...
2016: BMC Pediatrics
https://www.readbyqxmd.com/read/27581980/multiple-roles-of-the-cytoplasmic-domain-of-herpes-simplex-virus-1-envelope-glycoprotein-d-in-infected-cells
#17
Jun Arii, Keiko Shindo, Naoto Koyanagi, Akihisa Kato, Yasushi Kawaguchi
: Herpes simplex virus 1 (HSV-1) envelope glycoprotein D (gD) plays an essential role in viral entry. The functional regions of gD responsible for viral entry have been mapped to its extracellular domain, whereas the gD cytoplasmic domain plays no obvious role in viral entry. Thus far, the role(s) of the gD cytoplasmic domain in HSV-1 replication has remained to be elucidated. In this study, we show that ectopic expression of gD induces microvillus-like tubular structures at the plasma membrane which resemble the reported projection structures of the plasma membrane induced in HSV-1-infected cells...
November 15, 2016: Journal of Virology
https://www.readbyqxmd.com/read/27573107/platelet-derived-growth-factor-%C3%AE-receptor-is-the-cellular-receptor-for-human-cytomegalovirus-ghglgo-trimer
#18
Anna Kabanova, Jessica Marcandalli, Tongqing Zhou, Siro Bianchi, Ulrich Baxa, Yaroslav Tsybovsky, Daniele Lilleri, Chiara Silacci-Fregni, Mathilde Foglierini, Blanca Maria Fernandez-Rodriguez, Aliaksandr Druz, Baoshan Zhang, Roger Geiger, Massimiliano Pagani, Federica Sallusto, Peter D Kwong, Davide Corti, Antonio Lanzavecchia, Laurent Perez
Human cytomegalovirus encodes at least 25 membrane glycoproteins that are found in the viral envelope(1). While gB represents the fusion protein, two glycoprotein complexes control the tropism of the virus: the gHgLgO trimer is involved in the infection of fibroblasts, and the gHgLpUL128L pentamer is required for infection of endothelial, epithelial and myeloid cells(2-5). Two reports suggested that gB binds to ErbB1 and PDGFRα (refs 6,7); however, these results do not explain the tropism of the virus and were recently challenged(8,9)...
June 6, 2016: Nature Microbiology
https://www.readbyqxmd.com/read/27562261/structures-of-ebola-virus-gp-and-sgp-in-complex-with-therapeutic-antibodies
#19
Jesper Pallesen, Charles D Murin, Natalia de Val, Christopher A Cottrell, Kathryn M Hastie, Hannah L Turner, Marnie L Fusco, Andrew I Flyak, Larry Zeitlin, James E Crowe, Kristian G Andersen, Erica Ollmann Saphire, Andrew B Ward
The Ebola virus (EBOV) GP gene encodes two glycoproteins. The major product is a soluble, dimeric glycoprotein (sGP) that is secreted abundantly. Despite the abundance of sGP during infection, little is known regarding its structure or functional role. A minor product, resulting from transcriptional editing, is the transmembrane-anchored, trimeric viral surface glycoprotein (GP). GP mediates attachment to and entry into host cells, and is the intended target of antibody therapeutics. Because large portions of sequence are shared between GP and sGP, it has been hypothesized that sGP may potentially subvert the immune response or may contribute to pathogenicity...
2016: Nature Microbiology
https://www.readbyqxmd.com/read/27536733/hsv-2-%C3%AE-gd-elicits-fc%C3%AE-r-effector-antibodies-that-protect-against-clinical-isolates
#20
Christopher D Petro, Brian Weinrick, Nazanin Khajoueinejad, Clare Burn, Rani Sellers, William R Jacobs, Betsy C Herold
A single-cycle herpes simplex virus (HSV) deleted in glycoprotein D (ΔgD-2) elicited high titer HSV-specific antibodies (Abs) that (i) were rapidly transported into the vaginal mucosa; (ii) elicited antibody-dependent cell-mediated cytotoxicity but little neutralization; (iii) provided complete protection against lethal intravaginal challenge; and (iv) prevented establishment of latency in mice. However, clinical isolates may differ antigenically and impact vaccine efficacy. To determine the breadth and further define mechanisms of protection of this vaccine candidate, we tested ΔgD-2 against a panel of clinical isolates in a murine skin challenge model...
August 4, 2016: JCI Insight
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