Hybrid Polymeric Systems for Nano-Selective Counter Intervention in Virus Life Cycle

2010 ◽  
Vol 296 (1) ◽  
pp. 466-477 ◽  
Author(s):  
Alexander Serbin ◽  
Ekaterina Karaseva ◽  
Vladimir Tsvetkov ◽  
Olga Alikhanova ◽  
Igor Rodionov
Keyword(s):  
Life Cycle ◽  
Polymeric Systems ◽  
Virus Life Cycle

scholarly journals Role of Virally-Encoded Deubiquitinating Enzymes in Regulation of the Virus Life Cycle

2021 ◽  
Vol 22 (9) ◽  
pp. 4438
Author(s):  
Jessica Proulx ◽  
Kathleen Borgmann ◽  
In-Woo Park
Keyword(s):  
Immune Response ◽  
Life Cycle ◽  
Deubiquitinating Enzyme ◽  
Deubiquitinating Enzymes ◽  
Antiviral Immune Response ◽  
Cellular Processes ◽  
Virus Life Cycle ◽  
Infected Cells ◽  
Dependent Processes

The ubiquitin (Ub) proteasome system (UPS) plays a pivotal role in regulation of numerous cellular processes, including innate and adaptive immune responses that are essential for restriction of the virus life cycle in the infected cells. Deubiquitination by the deubiquitinating enzyme, deubiquitinase (DUB), is a reversible molecular process to remove Ub or Ub chains from the target proteins. Deubiquitination is an integral strategy within the UPS in regulating survival and proliferation of the infecting virus and the virus-invaded cells. Many viruses in the infected cells are reported to encode viral DUB, and these vial DUBs actively disrupt cellular Ub-dependent processes to suppress host antiviral immune response, enhancing virus replication and thus proliferation. This review surveys the types of DUBs encoded by different viruses and their molecular processes for how the infecting viruses take advantage of the DUB system to evade the host immune response and expedite their replication.

scholarly journals Multiple effects of toxins isolated from Crotalus durissus terrificus on the hepatitis C virus life cycle

PLoS ONE ◽  
2017 ◽  
Vol 12 (11) ◽  
pp. e0187857 ◽  
Author(s):  
Jacqueline Farinha Shimizu ◽  
Carina Machado Pereira ◽  
Cintia Bittar ◽  
Mariana Nogueira Batista ◽  
Guilherme Rodrigues Fernandes Campos ◽  
...  
Keyword(s):  
Life Cycle ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Crotalus Durissus Terrificus ◽  
Virus Life Cycle ◽  
Crotalus Durissus

scholarly journals Novel reporter system to monitor early stages of the hepatitis B virus life cycle

2015 ◽  
Vol 106 (11) ◽  
pp. 1616-1624 ◽  
Author(s):  
Hironori Nishitsuji ◽  
Saneyuki Ujino ◽  
Yuko Shimizu ◽  
Keisuke Harada ◽  
Jing Zhang ◽  
...  
Keyword(s):  
Life Cycle ◽  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Reporter System ◽  
Early Stages ◽  
Virus Life Cycle ◽  
B Virus

scholarly journals COVID-19 Docking Server: a meta server for docking small molecules, peptides and antibodies against potential targets of COVID-19

2020 ◽  
Vol 36 (20) ◽  
pp. 5109-5111 ◽  
Author(s):  
Ren Kong ◽  
Guangbo Yang ◽  
Rui Xue ◽  
Ming Liu ◽  
Feng Wang ◽  
...  
Keyword(s):  
Life Cycle ◽  
Drug Discovery ◽  
Small Molecules ◽  
Web Server ◽  
Supplementary Information ◽  
Binding Modes ◽  
Supplementary Data ◽  
Virus Life Cycle ◽  
Ligand Interactions ◽  
New Type

Abstract Motivation The coronavirus disease 2019 (COVID-19) caused by a new type of coronavirus has been emerging from China and led to thousands of death globally since December 2019. Despite many groups have engaged in studying the newly emerged virus and searching for the treatment of COVID-19, the understanding of the COVID-19 target–ligand interactions represents a key challenge. Herein, we introduce COVID-19 Docking Server, a web server that predicts the binding modes between COVID-19 targets and the ligands including small molecules, peptides and antibodies. Results Structures of proteins involved in the virus life cycle were collected or constructed based on the homologs of coronavirus, and prepared ready for docking. The meta-platform provides a free and interactive tool for the prediction of COVID-19 target–ligand interactions and following drug discovery for COVID-19. Availability and implementation http://ncov.schanglab.org.cn. Supplementary information Supplementary data are available at Bioinformatics online.

scholarly journals Scanning Mutagenesis Studies Reveal a Potential Intramolecular Interaction within the C-Terminal Half of Dengue Virus NS2A Involved in Viral RNA Replication and Virus Assembly and Secretion

2015 ◽  
Vol 89 (8) ◽  
pp. 4281-4295 ◽  
Author(s):  
Ren-Huang Wu ◽  
Ming-Han Tsai ◽  
Day-Yu Chao ◽  
Andrew Yueh
Keyword(s):  
Life Cycle ◽  
Dengue Virus ◽  
Virus Assembly ◽  
Intramolecular Interaction ◽  
Rna Replication ◽  
The Other ◽  
Amino Acid Residues ◽  
Wild Type ◽  
Transmembrane Segments ◽  
Virus Life Cycle

ABSTRACTThe NS2A protein of dengue virus (DENV) has eight predicted transmembrane segments (pTMSs; pTMS1 to pTMS8). NS2A has been shown to participate in RNA replication, virion assembly, and the host antiviral response. However, the role of the amino acid residues within the pTMS regions of NS2A during the virus life cycle is poorly understood. In the study described here, we explored the function of DENV NS2A by introducing a series of double or triple alanine substitutions into the C-terminal half (pTMS4 to pTMS8) of NS2A in the context of a DENV infectious clone or subgenomic replicon. Fourteen (8 within pTMS8) of 35 NS2A mutants displayed a lethal phenotype due to impairment of RNA replication by a replicon assay. Three NS2A mutants with mutations within pTMS7, the CM20, CM25, and CM27 mutants, displayed similar phenotypes, low virus yields (>100-fold reduction), wild-type-like replicon activity, and low infectious virus-like particle yields by transienttrans-packaging experiments, suggesting a defect in virus assembly and secretion. The sequencing of revertant viruses derived from CM20, CM25, and CM27 mutant viruses revealed a consensus reversion mutation, leucine (L) to phenylalanine (F), at codon 181 within pTMS7. The introduction of an L181F mutation into a full-length NS2A mutant, i.e., the CM20, CM25, and CM27 constructs, completely restored wild-type infectivity. Notably, L181F also substantially rescued the other severely RNA replication-defective mutants with mutations within pTMS4, pTMS6, and pTMS8, i.e., the CM2, CM3, CM13, CM31, and CM32 mutants. In conclusion, the results revealed the essential roles of pTMS4 to pTMS8 of NS2A in RNA replication and/or virus assembly and secretion. The intramolecular interaction between pTMS7 and pTMS4, pTMS6, or pTMS8 of the NS2A protein was also implicated.IMPORTANCEThe reported characterization of the C-terminal half of dengue virus NS2A is the first comprehensive mutagenesis study to investigate the function of flavivirus NS2A involved in the steps of the virus life cycle. In particular, detailed mapping of the amino acid residues within the predicted transmembrane segments (pTMSs) of NS2A involved in RNA replication and/or virus assembly and secretion was performed. A revertant genetics study also revealed that L181F within pTMS7 is a consensus reversion mutation that rescues both RNA replication-defective and virus assembly- and secretion-defective mutants with mutations within the other three pTMSs of NS2A. Collectively, these findings elucidate the role played by NS2A during the virus life cycle, possibly through the intricate intramolecular interaction between pTMS7 and other pTMSs within the NS2A protein.

scholarly journals Intracellular Expression of Camelid Single-Domain Antibodies Specific for Influenza Virus Nucleoprotein Uncovers Distinct Features of Its Nuclear Localization

2014 ◽  
Vol 89 (5) ◽  
pp. 2792-2800 ◽  
Author(s):  
Joseph Ashour ◽  
Florian I. Schmidt ◽  
Leo Hanke ◽  
Juanjo Cragnolini ◽  
Marco Cavallari ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Life Cycle ◽  
Nuclear Localization ◽  
Nuclear Import ◽  
Rna Viruses ◽  
Single Domain ◽  
Single Domain Antibody ◽  
Virus Life Cycle ◽  
Domain Antibody ◽  
Chemical Inhibition

ABSTRACTPerturbation of protein-protein interactions relies mostly on genetic approaches or on chemical inhibition. Small RNA viruses, such as influenza A virus, do not easily lend themselves to the former approach, while chemical inhibition requires that the target protein be druggable. A lack of tools thus constrains the functional analysis of influenza virus-encoded proteins. We generated a panel of camelid-derived single-domain antibody fragments (VHHs) against influenza virus nucleoprotein (NP), a viral protein essential for nuclear trafficking and packaging of the influenza virus genome. We show that these VHHs can target NP in living cells and perturb NP's function during infection. Cytosolic expression of NP-specific VHHs (αNP-VHHs) disrupts virus replication at an early stage of the life cycle. Based on their specificity, these VHHs fall into two distinct groups. Both prevent nuclear import of the viral ribonucleoprotein (vRNP) complex without disrupting nuclear import of NP alone. Different stages of the virus life cycle thus rely on distinct nuclear localization motifs of NP. Their molecular characterization may afford new means of intervention in the virus life cycle.IMPORTANCEMany proteins encoded by RNA viruses are refractory to manipulation due to their essential role in replication. Thus, studying their function and determining how to disrupt said function through pharmaceutical intervention are difficult. We present a novel method based on single-domain-antibody technology that permits specific targeting and disruption of an essential influenza virus protein in the absence of genetic manipulation of influenza virus itself. Characterization of such interactions may help identify new targets for pharmaceutical intervention. This approach can be extended to study proteins encoded by other viral pathogens.

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