Relevant bibliographies by topics / Structural virology

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Structural virology'

Author: Grafiati
Published: 14 December 2024

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Journal articles on the topic "Structural virology"

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Agbandje-McKenna, Mavis, and Richard Kuhn. "Current opinion in virology: structural virology." Current Opinion in Virology 1, no. 2 (August 2011): 81–83. http://dx.doi.org/10.1016/j.coviro.2011.07.001.

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Stuart, David. "Changing times in structural virology." Acta Crystallographica Section A Foundations and Advances 75, a2 (August 18, 2019): e18-e18. http://dx.doi.org/10.1107/s205327331909538x.

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Sousa, Rui. "Structural Virology 4. T7 RNA Polymerase." Uirusu 51, no. 1 (2001): 81–94. http://dx.doi.org/10.2222/jsv.51.81.

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Shepherd, C. M. "VIPERdb: a relational database for structural virology." Nucleic Acids Research 34, no. 90001 (January 1, 2006): D386—D389. http://dx.doi.org/10.1093/nar/gkj032.

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Kiss, Bálint, Dorottya Mudra, György Török, Zsolt Mártonfalvi, Gabriella Csík, Levente Herényi, and Miklós Kellermayer. "Single-particle virology." Biophysical Reviews 12, no. 5 (September 3, 2020): 1141–54. http://dx.doi.org/10.1007/s12551-020-00747-9.

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Abstract The development of advanced experimental methodologies, such as optical tweezers, scanning-probe and super-resolved optical microscopies, has led to the evolution of single-molecule biophysics, a field of science that allows direct access to the mechanistic detail of biomolecular structure and function. The extension of single-molecule methods to the investigation of particles such as viruses permits unprecedented insights into the behavior of supramolecular assemblies. Here we address the scope of viral exploration at the level of individual particles. In an era of increased awareness towards virology, single-particle approaches are expected to facilitate the in-depth understanding, and hence combating, of viral diseases.
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Meier, Kristina, Sigurdur R. Thorkelsson, Emmanuelle R. J. Quemin, and Maria Rosenthal. "Hantavirus Replication Cycle—An Updated Structural Virology Perspective." Viruses 13, no. 8 (August 6, 2021): 1561. http://dx.doi.org/10.3390/v13081561.

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Hantaviruses infect a wide range of hosts including insectivores and rodents and can also cause zoonotic infections in humans, which can lead to severe disease with possible fatal outcomes. Hantavirus outbreaks are usually linked to the population dynamics of the host animals and their habitats being in close proximity to humans, which is becoming increasingly important in a globalized world. Currently there is neither an approved vaccine nor a specific and effective antiviral treatment available for use in humans. Hantaviruses belong to the order Bunyavirales with a tri-segmented negative-sense RNA genome. They encode only five viral proteins and replicate and transcribe their genome in the cytoplasm of infected cells. However, many details of the viral amplification cycle are still unknown. In recent years, structural biology methods such as cryo-electron tomography, cryo-electron microscopy, and crystallography have contributed essentially to our understanding of virus entry by membrane fusion as well as genome encapsidation by the nucleoprotein. In this review, we provide an update on the hantavirus replication cycle with a special focus on structural virology aspects.
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Rossmann, Michael G. "Virus crystallography and structural virology: a personal perspective." Crystallography Reviews 21, no. 1-2 (November 14, 2014): 57–102. http://dx.doi.org/10.1080/0889311x.2014.957282.

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Khayat, Reza. "Call for Papers: Special Issue on Structural Virology." Viral Immunology 32, no. 10 (December 1, 2019): 415. http://dx.doi.org/10.1089/vim.2019.29046.cfp.

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Schoehn, Guy, Florian Chenavier, and Thibaut Crépin. "Advances in Structural Virology via Cryo-EM in 2022." Viruses 15, no. 6 (June 2, 2023): 1315. http://dx.doi.org/10.3390/v15061315.

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Dowd, Kimberly A., and Theodore C. Pierson. "The Many Faces of a Dynamic Virion: Implications of Viral Breathing on Flavivirus Biology and Immunogenicity." Annual Review of Virology 5, no. 1 (September 29, 2018): 185–207. http://dx.doi.org/10.1146/annurev-virology-092917-043300.

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Flaviviruses are arthropod-borne RNA viruses that are a significant threat to global health due to their widespread distribution, ability to cause severe disease in humans, and capacity for explosive spread following introduction into new regions. Members of this genus include dengue, tick-borne encephalitis, yellow fever, and Zika viruses. Vaccination has been a highly successful means to control flaviviruses, and neutralizing antibodies are an important component of a protective immune response. High-resolution structures of flavivirus structural proteins and virions, alone and in complex with antibodies, provide a detailed understanding of viral fusion mechanisms and virus-antibody interactions. However, mounting evidence suggests these structures provide only a snapshot of an otherwise structurally dynamic virus particle. The contribution of the structural ensemble arising from viral breathing to the biology, antigenicity, and immunity of flaviviruses is discussed, including implications for the development and evaluation of flavivirus vaccines.
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Dissertations / Theses on the topic "Structural virology"

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Sabaratnam, Keshalini. "The interaction between the Marek's Disease Virus (MDV) neurovirulence factor pp14 and the host transcription factor, CREB3." Thesis, University of Oxford, 2017. http://ora.ox.ac.uk/objects/uuid:d2fc6bd4-bc3a-4a37-924b-86881096a9b5.

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Marek's Disease Virus (MDV) induces a wide range of neurological syndromes in susceptible hosts; however, the mechanisms behind the MDV-induced neuropathology are still poorly understood. The immediate-early 14kDa phosphoprotein, pp14, is associated with the neurovirulence phenotype of the virus. Yeast-two-hybrid screening identified the ER-bound transcription regulator, human CREB3 (cAMP Response Element-Binding protein), as an interacting partner of pp14, and fluorescence colocalisation between pp14 and chicken CREB3 (chCREB3) in MDV infected cells suggested an interaction between these proteins. The primary focus of this DPhil project was to further investigate this putative interaction using in vitro studies, with a view to determining if the interaction is linked to the neurovirulence of MDV. This investigation, which employed a combination of biochemical, cellular, and functional assays, found no conclusive evidence in support of the predicted interaction. In addition, this project aimed to gain structural and functional insights into the MDV neurovirulence factor pp14 and the host transcription factor, chCREB3. Biophysical characterisation of recombinant pp14B identifies pp14 as a molten globule. The results reveal the protein, while possessing substantial secondary structure, is largely disordered lacking a stable tertiary structure. Multiple lines of evidence from this study also indicate pp14 is a putative zinc-binding protein. Moreover, phosphorylation analysis of recombinant pp14B, extracted from DF1 cells, by mass spectrometry provides conclusive evidence for the presence of two phosphorylation sites in the shared C-terminal region of pp14 - serines 72 and 76 of pp14B. Structural flexibility, through a lack of a definite ordered tertiary structure, and functional features that can induce structural modifications indicate pp14 might interact with a number of binding partners and therefore could play multiple roles during MDV infection - a strong possibility due to the expression of the protein in all the different stages of virus infection. Furthermore, this thesis presents the crystal structure of the homodimeric chCREB3 bZIP. The chCREB3 bZIP possesses a structured DNA binding region even in the absence of DNA, a feature that could potentially enhance both the DNA-binding specificity and affinity of chCREB3. Significantly, chCREB3 has a covalent intermolecular disulphide bond in the hydrophobic core of the bZIP, which may play a role in promoting stability. Moreover, sequence alignment of bZIP sequences from chicken, human and mouse reveals only members of the CREB3 subfamily possess this cysteine residue, indicating it could act as a redoxsensor. These results indicate members of the CREB3 subfamily, by possessing a putative redox-sensitive cysteine with the capacity to form an intermolecular disulphide bond, may be activated in response to oxidative stress.
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Conley, Michaela Jayne. "Structural and functional characterisation of feline calicivirus entry." Thesis, University of Glasgow, 2018. http://theses.gla.ac.uk/8920/.

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The Caliciviridae are a group of small, non-enveloped viruses with a positive sense, single stranded RNA genome. Caliciviruses include the noroviruses, responsible for winter vomiting disease, as well as several important veterinary pathogens. Feline calicivirus (FCV) is an excellent model for studying calicivirus entry, having a known protein receptor and being readily propagated in cell culture. Here we explore calicivirus entry, using FCV. Virus entry is the critical first step of infection and is therefore an important area of study. Both alpha 2-6 linked sialic acid and feline junctional adhesion molecule A (fJAM-A) have been identified as receptors for FCV. The attachment of FCV to fJAM-A, is followed by uptake via clathrin mediated endocytosis. Little is known, however, on the viral escape mechanism leading to delivery of the viral RNA into the cytoplasm. We set out to explore the nature of FCV attachment and uncoating using structural, biochemical and biophysical analyses. By cryogenic electron microscopy we have characterized the virus-receptor interaction at high-resolution. Using electron microscopy and an RNA release assay, we have investigated virion uncoating. Finally, we have explored the importance of receptor glycosylation, and oligomerisation. Our analysis has allowed us to construct an atomic model of the major capsid protein VP1. Upon binding to fJAM-A, FCV undergoes a conformational change (rotation and tilting of the capsomeres). Flexibility in the receptor decorated virion has prevented high-resolution structure analysis of the conformational change or the virus-receptor interaction. We have, however, seen that the structural changes are limited to the capsid spikes. We hypothesised that the conformational change may be a priming step that would prepare the virus for uncoating upon internalisation. We found that upon lowering the pH below 5, receptor decorated virions disassembled, supporting this hypothesis. Disassembly of the virus-receptor complex at low pH presented a tool for estimating the quantity of receptor needed to prime the capsid for uncoating. Cryo-EM studies reveal that FCV bound fJAM-A is monomeric although the receptor was found to be dimeric in solution as previously described for the human and murine homologues. Furthermore, it is hypothesised that this is the form found at tight junctions between cells. We propose that disruption of fJAM-A homodimers may be the mechanism by which induction of viral uptake by endocytosis is triggered. Finally, we have confirmed the presence of an N-linked glycosylation on fJAM-A and show that the removal of this carbohydrate moiety does not affect viral binding in vitro.
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Thompson, Catherine Isabelle. "Protein interaction studies on the rotavirus non-structural protein NSP1." Thesis, University of Warwick, 1999. http://wrap.warwick.ac.uk/80266/.

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Rotavirus encodes six structural and six non-structural proteins. In contrast to the structural proteins, the functional roles of the non-structural proteins are not well defined beyond a realisation that they must have a role in the viral replication cycle. A fuller understanding of the replication cycle must therefore rest on determining the specific roles played by the non-structural proteins. Non-structural protein NSP1 shows high levels of sequence divergence. A generally well conserved cysteine-rich region at the amino-terminus may form a zinc finger structure. It has been shown to possess non-specific RNA-binding activity, and has been found associated with the smallest of three replication intermediates (RIs) found in infected cells, together with the viral proteins VP1, VP3 and NSP3. VP2 and VP6 are added sequentially to the pre-core RI to form the core RI and single-shelled RI respectively. The function of NSP1 in the replication cycle and the importance of its presence in early replication complexes has not been determined. The intermolecular interactions that occur between the components of the RIs have not been defined. Protein-protein interactions between NSP1 and VP1, VP2, VP3, and NSP3, from the UKtc strain of bovine rotavirus, were investigated using a variety of approaches, the first of which was the yeast two-hybrid system. In this assay a self-interaction of NSP1 was not detected. Protein-protein interactions between NSPl and VPl, VP2, VP3, and NSP3, were also not detected. Both the full-length protein and a truncated NSPl, consisting of only the amino terminal third of the protein, were tested. A direct self-interaction of NSP3 was shown and quantified. Radio-immunoprecipitation analysis of in vitro translated viral proteins using specific anti-NSP1 serum was also employed. However, it failed to detect direct protein-protein interactions between NSP1 and VPI, VP2, and VP3. Immunoprecipitation of UKtc rotavirus-infected celllysates with anti-NSP1 serum showed the co-precipitation of viral proteins VPl, VP2, VP3NP4, VP6 and NSP3, with NSP1. It was proposed that NSP1 formed a previously unrecognised complex with these proteins. Immunoprecipitation of nuclease-treated infected cell lysates showed a reduction in the co-precipitation of VP2, VP3NP4 and NSP3 with NSP1. No reduction in the co-precipitation of VP6 was seen. The association of the complex proteins may be mediated by RNA binding. Immunoprecipitation with an anti-VP6 monoclonal antibody reciprocally precipitated small amounts of NSP1, VP2, VP3/VP4, and NSP3, with VP6.
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Rezelj, Veronica Valentina. "Characterization of the non-structural (NSs) protein of tick-borne phleboviruses." Thesis, University of Glasgow, 2017. http://theses.gla.ac.uk/8149/.

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In recent years, a number of newly discovered tick-borne viruses exhibiting a wide spectrum of diseases in humans have been ascribed to the Phlebovirus genus of the Bunyaviridae family. These viruses have a tripartite RNA genome composed of two negative-sense RNA segments (medium and large) and one ambisense segment (small), which encode four structural proteins and one non-structural protein (NSs). The NSs protein is the major virulence factor of bunyaviruses, and acts as an antagonist of a key component of the first line of defence against viral infections: the interferon (IFN) system (Bridgen et al., 2001; Weber et al., 2002). The work presented herein describes the characterization of tick-borne phlebovirus NSs proteins as IFN antagonists. The development of a reverse genetics system for the apathogenic tick-borne Uukuniemi phlebovirus (UUKV) enabled the recovery of infectious UUKV entirely from cDNA. A recombinant UUKV lacking NSs induced higher amounts of IFN in infected cells compared to wild-type UUKV, suggesting a role of NSs in modulating the IFN response. The weak IFN antagonistic activity of UUKV NSs was evident using transient transfection reporter assays in comparison to the NSs protein of either pathogenic Heartland virus (HRTV) or Severe fever with thrombocytopenia syndrome virus (SFTSV). The sensitivity of UUKV, HRTV and SFTSV to exogenous and virus-induced IFN, as well as their growth kinetics in IFN-competent cells were examined. The molecular mechanisms employed by UUKV, HRTV and SFTSV NSs proteins to evade antiviral immunity were investigated using reporter assays, immunofluorescence, and immunoprecipitation studies. Collectively, these assays showed that UUKV NSs was able to weakly inhibit IFN induction but not IFN signalling, through a novel interaction with MAVS (mitochondrial antiviral signalling protein). On the other hand, HRTV and SFTSV NSs proteins potently inhibited IFN induction through an interaction with TBK1, and type I but not type II IFN signalling via an interaction with STAT2. Finally, the development of a minigenome system for HRTV in conjunction with minigenomes developed for UUKV and SFTSV (Brennan et al., 2015) provided preliminary data to assess possible outcomes of tick-borne phlebovirus reassortment. In summary, the results described in this thesis offer insights into how tick-borne phlebovirus pathogenicity may be linked to the capacity of their NSs proteins to block the innate immune system. The data presented also illustrate the plethora of viral immune evasion strategies utilized by emerging phleboviruses, and provide an insight into the possibility of tick-borne phlebovirus reassortment.
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Howard, Susan Teresa. "Structural and functional analyses on the SalI G fragment of vaccinia virus." Thesis, University of Cambridge, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.386088.

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Martin, Morgan Mackensie. "Functional analysis of hepatitis C virus non-structural protein (NS) 3 protease and viral cofactor NS4A." Thesis, University of British Columbia, 2008. http://hdl.handle.net/2429/1522.

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The hepatitis C virus (HCV) was identified in 1989 as the major causative agent of transfusion-associated non-A, non-B hepatitis and today represents a worldwide health crisis with prevalence estimates of 2.2%. HCV-specific therapeutics have never been more urgently needed. One of the validated drug targets is the non-structural (NS) protein 3 (NS3) membrane-bound protease. The major aim of this thesis was characterization of NS3 allosteric activation by its viral cofactor, NS4A. We hypothesized that there would be specific residues that dominate the interaction between NS3 and NS4A, and further hypothesized that binding and activation may be separate events mediated by different residues. This thesis details the development of novel cell-based assays for detection of NS3-4A protease activity and heterocomplex formation. The protease assay substrate was a membrane-targeted intracellular protein, which upon proteolysis released a red fluorescent protein (FP) reporter, DsRed-Express, into the cytoplasm; this change was detected by microscopy or quantified by Western blotting. The complex formation assay detected fluorescence resonance energy transfer (FRET) between yellow and cyan FP-tagged NS3 and NS4A, respectively. Our data shows binding can be functionally separated from activation. We identified two NS4A residues (I25 and I29) important for NS3 binding and two NS4A residues (V23 and I25) important for NS3 activation. Therefore the binding-pockets of these residues are prime targets for small-molecule therapeutic development. In addition, I have compared the NS3-4A substrate sequence cleavage efficiencies in vivo. I have been able to show that the activation-dependent NS4B/NS5A junction is processed efficiently and the NS4A/NS4B junction is not. I have also shown NS3-4A substrate specificity is not modulated by replicase components; however the specific activity of this enzyme is increased. The strength of this thesis work stems from the novel and creative development of cell-based assays that can easily be modified to study other membrane-associated proteases. In vitro assays fall short in that they do not take into account the unique micro-environment in which these proteases are found.
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Lauder, Rebecca Pink. "Structural analysis of adenovirus bound to blood coagulation factors that influence viral tropism." Thesis, University of Glasgow, 2011. http://theses.gla.ac.uk/2636/.

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Adenoviruses are currently the most commonly used vectors for clinical gene therapy trials. Of these, Ad5 is the most commonly used serotype. Upon intravenous delivery, the vectors are sequestered in the liver which reduces their efficacy. While the coxsackievirus and adenovirus receptor is responsible for in vitro cell entry, this pathway is not used in vivo. Blood coagulation factors have been implicated in mediating in vivo hepatic transduction, and it is therefore important to characterise the interaction between these and Ad5 in order to permit development of more efficacious and safer viral vectors. Ad35 is a rare human pathogen and presents less pre-existing immunity than Ad5 and other common serotypes. It has potential as a gene therapy vector as this may reduce side effects and toxicity linked to pre-existing immunity. Ad35 uses CD46 as a receptor instead of CAR which allows it to infect hepatocytes, however blood coagulation factor X has also been implicated in in vivo hepatic transduction. This interaction must therefore also be characterised. We used low dose cryo electron microscopy to collect images of Ad5, Ad5 bound to FX and to FIX, Ad35 and Ad35 bound to FX. These were used to generate three dimensional icosahedral reconstructions of Ad5 at 27Å, Ad5 bound to FX at 26Å and 14Å, Ad5 bound to FIX at 21Å, Ad35 at 35Å and Ad35 bound to FX at 30Å. High resolution structural data were fitted to the Ad5 and Ad5-FX reconstructions in order to model the interaction and identify the binding sites. The structural data presented show that FX binds to Ad5 hexon with a stoichiometry of 1/3. Fitting experiments showed that the Gla domain of FX corresponds with the density in the centre of the hexon trimer, with arms corresponding to the EGF domains extending from this and terminating in the globular serine protease domain. Furthermore FX binds to Ad35 hexon in a similar manner. The data also shows that FIX does not bind to Ad5 hexon, however we were unable to confirm it if instead binds to the fiber as suggested by biochemical studies, due to limitations in the reconstruction technique used.
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Leigh, Kendra Elizabeth. "Structural Studies of a Subunit of the Murine Cytomegalovirus Nuclear Egress Complex." Thesis, Harvard University, 2015. http://nrs.harvard.edu/urn-3:HUL.InstRepos:14226065.

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The Herpesviridae family of viruses includes a number of human pathogens of clinical importance. Like other herpesviruses, cytomegaloviruses require a heterodimeric nuclear egress complex (NEC) consisting of a membrane-bound protein and a soluble nucleoplasmic protein, termed in murine cytomegalovirus (MCMV) M50 and M53, respectively. Genetic, electron microscopic, and immunocytochemical studies have revealed the importance of this complex for viral replication, most predominantly in facilitating egress of viral nucleocapsids across the nuclear membrane. Despite the significance of the NEC to the herpesvirus life cycle, there is a dearth of structural information regarding the components of the complex. We present here an NMR-determined solution-state structure of the conserved, structured, soluble portion of M50 (residues 1-168), which exhibits novel structural character. We mapped the binding site of a highly conserved minimal binding domain of the M53 homologue from human cytomegalovirus (HCMV; UL53) required for heterodimerization onto the structure and identified specific residues in a groove within the M50 protein fold that interact with the UL53 peptide. This site was verified biophysically and biologically: single amino acid substitutions of the corresponding residues of the homologous protein from HCMV (UL50) resulted in decreased UL53 binding in vitro, as measured by isothermal titration calorimetry, and substitutions that had the greatest effect on binding affinity caused disruption of UL50-UL53 co-localization and lethal defects in the context of HCMV infection. We then compared the effect of binding UL53 peptide with binding of the larger natural binding partner, M53 (residues 103-333) via NMR, with the results suggesting that conformational changes most likely occur on a fold-wide level in the context of the full complex. We suggest that these findings combined with the clinical relevance, the virus-specific aspects of nuclear egress, and the novelty of the structure make the HCMV NEC an attractive potential drug target. To this end, we used in silico screening to identify possible small molecule inhibitors and have begun validating top screen hits biophysically and biologically.
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Ruiz, Arroyo Víctor Manuel. "Structural and functional analysis of Zika Virus NS5 protein." Doctoral thesis, Universitat de Barcelona, 2020. http://hdl.handle.net/10803/671922.

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Zika virus (ZIKV) belongs to the Flaviviridae family and constitute an important public health concern since ZIKV infection produced devastating effects in new born infants. Flaviviruses present a positive sense single stranded RNA genome flanked by highly structured untranslated regions (UTR) carrying one open reading frame that codifies for three structural proteins (C, prM, E) and five nonstructural proteins (NS1-5). At the most C-terminal end, NS5 protein carries a RNA dependent RNA polymerase (RdRP) and a methyl transferase domain (MTase) for genome copying and 5’ capping activities of the newly synthesized RNA, respectively. Given the crucial role of this enzyme for viral replication, NS5 constitutes an attractive antiviral target to inhibit viral replication. In this study, we determined the structure of the ZIKV NS5 protein using X-Ray crystallography combined with several structural biology approaches to characterize the supramolecular arrangement of the ZIKV NS5 protein. We identified the monomer-monomer and dimer-diner interactions to form fibril-like structures, and evaluated the role of oligomer formation, using in-vitro polymerization assays. We also evaluated the in-vivo effect of NS5-oligomerisation in chicken embryos, stablishing a connection between this protein and microcephaly. One of the most important RNA structures present at the 5’UTR of flavivirus genomes is the 5SLA. This structure was identified previously to bind the NS5 protein, acting as a promoter and being essential for viral replication. We assayed and optimized the NS5-5SLA complex stability using biophysical and biochemical techniques and determined the structure of the complex by single particle cryo-EM. Comparisons between the NS5-5SLA complex and the NS5 crystallographic structure revealed for the first time in flavivirus, important conformational changes in the NS5 RdRP. We identified the residues involved in complex formation and characterized the effect of this binding on NS5 polymerization, shedding new light on the understanding of replication mechanisms in flaviviruses.
El virus Zika (ZIKV) pertenece a la familia Flaviviridae y constituye una amenaza para la salud pública, especialmente debido a las malformaciones provocadas en neonatos. Los flavivirus presentan un genoma RNA de simple cadena con polaridad positiva, flanqueado por regiones no traducidas (UTR) que presentan una elevada estructura secundaria, seguido de una región codificante para una única poliproteína que por proteólisis dará lugar a tres proteínas estructurales (C, prM, E) y cinco proteinas no estructurales (NS1-5). En el extremo C-terminal se encuentra la proteina NS5 que presenta actividad ARN polimerasa dependiente de ARN (RdRP) y un dominio metil-transferasa (MTase) para copiar el genoma y añadir una caperuza al extremo 5’ del nuevo ARN sintetizado, respectivamente. Dado el papel crucial de este enzima en la replicación viral, la proteina NS5 constituye una diana antiviral muy atractiva para inhibir la replicación del virus. En este estudio, determinamos la estructura de la proteína NS5 de ZIKV, usando cristalografía de Rayos-X combinada con diferentes técnicas biofísicas para caracterizar la organización supramolecular de la proteína. Identificamos las interacciones monomero-monomero y dimero-dimero para caracterizar las estructuras fibrilares de la proteína y evaluamos los efectos de la dimerización en la actividad polimerasa in-vitro. También evaluamos los efectos de la oligomerización de NS5 in-vivo en embriones de pollo, estableciendo una conexión entre esta proteína y la aparición de microcefalia en fetos infectados. Una de las estructuras de ARN más importantes presentes en el 5’UTR del genoma de los flavivirus es el 5SLA. Previamente se describió que esta estructura se unía a NS5 y actuaba como un promotor, siendo ademas esencial para la replicación viral. Medimos y optimizamos la estabilidad del complejo NS5-5SLA mediante técnicas biofísicas y bioquímicas y determinamos la estructura del complejo mediante cryo-EM. Las comparaciones entre la estructura cristalográfica y cryo-EM de NS5 revelaron, por primera vez en flavivirus, cambios conformacionales importantes en el dominio RdRP. Identificamos los residuos implicados en la formación del complejo y caracterizamos el efecto de la unión de NS5 a 5SLA sobre su actividad polimerasa. Estos resultados arrojan nueva luz para entender los mecanismos de replicación en los flavivirus.
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Rainsford, Edward. "Functional studies on the rotavirus non-structural proteins NSP5 and NSP6." Thesis, University of Warwick, 2005. http://wrap.warwick.ac.uk/53876/.

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The rotavirus replication cycle has not been fully characterised, one vital stage of virus replication involves large cytoplasmic occlusion bodies termed viroplasms. These are the sites of synthesis and replication of dsRNA, packaging of viral RNA into newly synthesized cores and the formation of double-shelled previrions. The detailed mechanism by which these events occur is poorly understood but is thought to be mediated by the non-structural proteins localised to these structures. Rotavirus gene segment 11 expresses two proteins NSP5 and NSP6 which are found in alternate open reading frames. NSP5 exists is several isoforms which differ on their level of phosphorylation. It has been shown to be essential for virus replication and localises to the viroplasms. The smaller NSP6 protein is the most uncharacterised of all of the rotavirus proteins. It has however been shown to interact with NSP5 and has been tentatively suggested to be localised to the viroplasms. To further investigate these two proteins the pET expression system was utilised to obtain purified protein which was subsequently used to generate mono specific polyclonal antisera. Studies into the function and localisation of these proteins found that both localised to the viroplasms and their relative distributions within these structures were defined. NSP6 was found to be expressed at a low level throughout the course of a rotavirus infection and in contrast to other non-structural proteins, to have a high rate of turnover. The RNA binding ability of both NSP5 and NSP6 was investigated using quantitative filter binding assays and these showed both have sequence independent nucleic acid binding ability. Studies were also conducted into the mechanism of NSP6 expression from the second open reading frame of gene 11, the results obtained being consistent with a leaky scanning mechanism of expression.
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Books on the topic "Structural virology"

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Agbandje-McKenna, Mavis, and Robert McKenna, eds. Structural Virology. Cambridge: Royal Society of Chemistry, 2010. http://dx.doi.org/10.1039/9781849732239.

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Agbandje-McKenna, Mavis, and McKenna Robert. Structural virology. Cambridge: RSC Publishing, 2011.

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Uversky, Vladimir N. Flexible viruses: Structural disorder in viral proteins. Hoboken: Wiley, 2012.

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J, Gibbs A., Calisher Charles H, and Garcia-Arenal Fernando, eds. Molecular basis of virus evolution. Cambridge [England]: Cambridge University Press, 1995.

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Wah, Chiu, Burnett Roger M, and Garcea Robert L, eds. Structural biology of viruses. New York: Oxford University Press, 1997.

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Kasteel, Daniella T. J. Structure, morphogenesis and function of tubular structures induced by cowpea mosaic virus. Wageningen: [s.n.], 1999.

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McKenna, Robert, Stephen Neidle, David M. J. Lilley, Mavis Agbandje-McKenna, and Roderick E. Hubbard. Structural Virology. Royal Society of Chemistry, The, 2010.

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Longhi, Sonia, and Vladimir Uversky. Flexible Viruses: Structural Disorder in Viral Proteins. Wiley & Sons, Incorporated, John, 2011.

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Longhi, Sonia, and Vladimir Uversky. Flexible Viruses: Structural Disorder in Viral Proteins. Wiley & Sons, Incorporated, John, 2011.

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Longhi, Sonia, and Vladimir Uversky. Flexible Viruses: Structural Disorder in Viral Proteins. Wiley & Sons, Incorporated, John, 2011.

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Book chapters on the topic "Structural virology"

1

Azad, Kimi, Debajit Dey, and Manidipa Banerjee. "Structural Alterations in Non-enveloped Viruses During Disassembly." In Physical Virology, 177–214. Cham: Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-36815-8_9.

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Schmidt, I., D. Ebner, M. A. Skinner, M. Pfleiderer, B. Schelle-Prinz, and S. G. Siddell. "Structural Proteins of the Murine Coronavirus MHV-JHM." In Modern Trends in Virology, 75–82. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73745-9_9.

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Bakshi, Arindam, G. P. Vishnu Vardhan, M. Hema, M. R. N. Murthy, and H. S. Savithri. "Structural and Functional Characterization of Sesbania Mosaic Virus." In A Century of Plant Virology in India, 405–27. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-5672-7_18.

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Fabian, Marc R., and K. Andrew White. "Solution Structure Probing of RNA Structures." In Plant Virology Protocols, 243–50. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-102-4_17.

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McGarvey, Michael J., and Michael Houghton. "Structure and Molecular Virology." In Viral Hepatitis, 219–45. Oxford, UK: John Wiley & Sons, Ltd, 2013. http://dx.doi.org/10.1002/9781118637272.ch16.

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Negro, Francesco. "Structure and Molecular Virology." In Viral Hepatitis, 393–402. Oxford, UK: John Wiley & Sons, Ltd, 2013. http://dx.doi.org/10.1002/9781118637272.ch27.

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Meng, Xiang-Jin. "Structure and Molecular Virology." In Viral Hepatitis, 417–30. Oxford, UK: John Wiley & Sons, Ltd, 2013. http://dx.doi.org/10.1002/9781118637272.ch30.

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Luangsay, Souphalone, and Fabien Zoulim. "Structure and Molecular Virology." In Viral Hepatitis, 63–80. Oxford, UK: John Wiley & Sons, Ltd, 2013. http://dx.doi.org/10.1002/9781118637272.ch5.

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Modrow, Susanne, Dietrich Falke, Uwe Truyen, and Hermann Schätzl. "Viruses: Definition, Structure, Classification." In Molecular Virology, 17–30. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-20718-1_2.

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Mateu, Mauricio G. "Virus Mechanics: A Structure-Based Biological Perspective." In Physical Virology, 237–82. Cham: Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-36815-8_11.

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Conference papers on the topic "Structural virology"

1

Lee, Junghoon, Peter C. Doerschuk, and John E. Johnson. "Simultaneous 3-D Image Reconstruction and Classication with Applications to Structural Virology*." In Signal Recovery and Synthesis. Washington, D.C.: OSA, 2007. http://dx.doi.org/10.1364/srs.2007.ptua1.

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Khalid MOHAMMED, Ansam, Nazih Wayes ZAID, and Mariam Hamdi ABDULKAREEM. "SECTION OF VETERINARY MEDICINE: MICROBIOLOGY, IMMUNITY AND VIROLOGY. THE BACTERIAL CONTAMINATION WITH PROTEUS AND E. COLI IN CERVIX AND UTERINE OF COWS DURING THE DIFFERENT ESTRUS PHASES." In VIII.International ScientificCongressofPure,AppliedandTechnological Sciences. Rimar Academy, 2023. http://dx.doi.org/10.47832/minarcongress8-15.

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Abstract:
The herein research was carried out in order to identified the presence of bacteria in cervix and uterine lumen in Iraqi cattle during the different estrus phase with focusing on Protus and E coli. Estrus phases were determined by the structures which found on ovary (follicular growth for pro-estrus, mature growing follicle for estrus, hemorrhagic corpus luteam for meta-estrus and active corpus luteam for di-eatrus). Forty cervical swabs (ten for each estrus phase) and forty uterine swabs (ten for each estrus phase) were taken from macroscopically healthy reproductive animals after slaughtering and cultivated on nutrient agar and blood agar, the bacterial isolation were identified with biochemical teats. The present study found that (65%) of cervical swabs were bacterial positive and the bacterial isolates were higher in the pro-estrus and meta-estrus phases 70% than estrus and diestrus 60%, the Protus spp. Could not been isolated from cervix or uterine during estrus phases, while E coli isolated during three first phases and disappear during diestrus phase, and appear as 10 single and 10 mixed isolated during follicular phase and metaestrus phase in cervical swabs. A total of five different microorganisms were isolated from cervical swabs (Escherichia coli, Streptococcus faecalis, Staphylococcus aureus, Staphylococcus hominies and Staphylococcus epidermidis) with twelve single isolation and fourteen mixed isolation. The present study found that (47.5%) of uterine swabs were bacterial positive and the bacterial isolates were higher in the pro-estrus, estrus and meta-estrus phases 50% than estrus and diestrus 40%, E coli isolated during estrus and diestrus phases only, and appear as 7 single and 2 mixed isolated during those two phases in uterine swabs. A total of five different microorganisms were isolated from uterine swabs (Escherichia coli, Streptococcus faecalis, Staphylococcus aureus, Staphylococcus hominies and Staphylococcus epidermidis) with fourteen single isolation and five mixed isolation.
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