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Wyszukujesz frazę "HSV-1" wg kryterium: Temat


Wyświetlanie 1-4 z 4
Tytuł:
Fold recognition insights into function of herpes ICP4 protein
Autorzy:
Wyrwicz, Lucjan
Rychlewski, Leszek
Powiązania:
https://bibliotekanauki.pl/articles/1040938.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
VZV
HSV2
Herpesviridae
bioinformatics
HSV1
ICP4 transcription regulator
Opis:
ICP4 is an important factor regulating the life cycle of HSV1. This conserved protein has several molecular functions, including activation of expression of viral late gene transcripts and inhibition of immediate early genes. Although ICP4 and its Alphaherpesvirinae homologs (eg.: IE62 of VZV) have been subjects of various molecular studies, a complete view of their molecular function is lacking. Here we present the results of fold recognition and molecular modelling of ICP4 functional domains. The performed state-of-the-art bioinformatic fold recognition analysis identified a dual helix-turn-helix motif as a binding module of repressor activities (so called region 2 domain). The mapping of distant homology identified that a segment responsible for activation of late gene promoters (region 4) exhibits folding of uracil DNA glycosylase (UDG), but seems to be a non-functional homolog of UDG. Potential implications of the results are discussed.
Źródło:
Acta Biochimica Polonica; 2007, 54, 3; 551-559
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Homologues of HSV-1 nuclear egress factor UL34 are potential phosphoinositide-binding proteins
Autorzy:
Wyrwicz, Lucjan
Koczyk, Grzegorz
Rychlewski, Leszek
Powiązania:
https://bibliotekanauki.pl/articles/1040842.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
HSV-1
Herpesviridae
phosphoinositides
protein structure prediction
bioinformatics
UL34
nuclear egress
Opis:
During the herpesvirus replication cycle, viral transcription, DNA replication, formation of capsids and DNA packaging occur in the nucleus. The subsequent nuclear egress of newly synthesized nucleocapsids is performed by budding of the inner leaflet of the nuclear membrane, which creates the primary envelope. Although products of two genes conserved throughout the Herpesviridae family (HSV-1 UL34 and UL31) have previously been shown to be involved in the execution of this process, the molecular basis of their activity is not clear. Here we present results of protein structure prediction for the conserved domain of UL34. The applied methodology suggests that this protein adopts a pleckstrin homology (PH) fold to perform its function. A detailed inspection of the ligand binding site strongly supports the hypothesis that UL34 orthologs can recognize phosphoinositides. Since previous works suggest that alterations of UL34 gene product result in a drastic impairment of primary envelopment of HSV-1 and trapping of capsids in the nucleus, the presented data may lead to the development of novel anti-herpetic therapeutic strategies where analogs of phosphoinositides are administered.
Źródło:
Acta Biochimica Polonica; 2008, 55, 1; 207-213
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Antiviral Activities of Cu2+ Ions in Viral Prevention, Replication, RNA Degradation, and for Antiviral Efficacies of Lytic Virus, ROS-Mediated Virus, Copper Chelation
Autorzy:
Ishida, Tsuneo
Powiązania:
https://bibliotekanauki.pl/articles/1177808.pdf
Data publikacji:
2018
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Tematy:
Capsid protein
Copper chelation
Copper homeostasis
Copper oxide nanoparticles
Cu2+ and Cu1+ ions
DNA/RNA virus
HSV
ROS
Viral replication
mRNA degradation or decay
Opis:
Copper has been known for decades that marked changes of micronutrient homeostasis in the host are accompanied by infection or inflammation. Copper levels in the serum are significantly elevated in response to inflammation that copper accumulates at sites of inflammation. Easily oxidized copper oxide nanoparticles (CuONPs) are widely used as catalysts that the ability of CuONPs to reduce bacterial population and virus application is enhanced. The mechanism of copper-mediated inactivation of herpes simplex virus (HSV) is by which cupric ions oxidatively damage biomolecules. Virus-mediated subjugation and modulation of host lipids during infection that the life cycle of most viruses proceeds through a series of basic steps: binding and internalization, fusion, uncoating, of the viral genome, its replication, assembly of new particles, and budding or release of the newly made viruses. The HIV-1 protein Vpu is an 81-amino-acid (16-kDa) type I which the presence of Vpu leads to the degradation of BST-2 via an endosome-lysosome degradation pathway. Oxidative degradation by a Cu-metalloenzyme, and ubiquitin-mediated degradation of cellular proteins were exploited. Copper can disrupt the lytic cycle of the Coccolithovirus. Lysins represent a novel class of anti-infectives derived from bacteriophage which lysins are bacterial cell wall hydrolytic enzymes that selectively and rapidly kill specific bacteria. Regarding copper induced cellular toxicity, several mechanisms have been proposed based on the formations of ROS by free Cu ions as cupric and cuprous ions can participate in redox reactions. ROS (O2ˉ,・OH, OHˉ), Cu+ and H2O2 play the important roles for viral inactivations. Thujaplicin-copper chelates inhibit influenza virus-induced apoptosis. Pyrrolidine dithiocarbamate as a metal ion binding agent inhibits the activity of the viral proteases of polyprotein processing and RNA replication of HRV. Chelation enables metals are capable of ligand scavenging via complexation, since reverse transcriptase enzyme inhibits the growth and replication of RNA tumor viruses. Thus, copper complex and copper chelation enhance antiviral efficacy.
Źródło:
World Scientific News; 2018, 99; 148-168
2392-2192
Pojawia się w:
World Scientific News
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-4 z 4

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