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Exploring novel strategies targeting HBV
Šmilauerová, Kristýna ; Grantz Šašková, Klára (advisor) ; Černý, Jan (referee)
An effective and safe vaccine against Hepatitis B virus already exists, yet morbidity and mortality of this illness are still high. The key to developing a reliable treatment is a deep knowledge of the virus' life cycle and functions of all its components. In the presented work we explored an interactome of the Core protein of the Hepatitis B virus. Using proximity-dependent biotin identification technique (BioID) coupled to mass spectrometry we have identified a list of potential candidates that are either significantly enriched (in total 105 proteins) or less abundant in the presence of the HBV Core protein in the cell (40 proteins). The list also includes known HBV Core interacting proteins SRPK1 and SRPK2, and p53 protein whose expression is known to be repressed due to the HBV Core interaction with the E2F1 transcription factor. Many of the newly identified possible HBV Core interacting proteins are involved in biological processes already known or are suspected to be influenced by the HBV such as translational and transporting processes or gene expression and macromolecule production. Overall, this work comprehensively characterizes the interaction landscape of the HBV Core protein in the live cells and might thus serve as a reliable start for in depth HBV-host interaction analysis. Key...
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The role of capsid protein in hepatitis B virus life cycle
Eliáš, Vratislav ; Weber, Jan (advisor) ; Drda Morávková, Alena (referee)
Hepatitis B virus (HBV) can cause either an acute or a chronic infection of hepatocytes, often leading to a hepatocellular carcinoma or a liver cirrhosis. HBV encodes seven proteins in its 3.2kb genome. Two of these proteins are transcribed from the same ORF (HBcAg and HBeAg). HBeAg, as a soluble variant of the core protein, plays a crucial role in virus immunogenicity. HBcAg, apart from building viral capsid, represents a pleiotropic protein engaging in multiple viral stages. Its primary structure is divided into two domains: an assembly domain and a C-terminal domain (CTD). The latter, containing four arginine clusters, is an important life cycle regulation element. By interaction with multiple viral and cellular factors, it directs the virus through a successful replication. In this thesis, we have collected the available data about the various roles of HBcAg in viral life cycle. We believe that further investigation of this field could lead to therapeutic advances resulting in the decrease of HBV infections worldwide, subsequently to a lower lethality connected with the diseases caused by HBV. Powered by TCPDF (www.tcpdf.org)
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Exploring novel strategies targeting HBV
Šmilauerová, Kristýna ; Grantz Šašková, Klára (advisor) ; Černý, Jan (referee)
An effective and safe vaccine against Hepatitis B virus already exists, yet morbidity and mortality of this illness are still high. The key to developing a reliable treatment is a deep knowledge of the virus' life cycle and functions of all its components. In the presented work we explored an interactome of the Core protein of the Hepatitis B virus. Using proximity-dependent biotin identification technique (BioID) coupled to mass spectrometry we have identified a list of potential candidates that are either significantly enriched (in total 105 proteins) or less abundant in the presence of the HBV Core protein in the cell (40 proteins). The list also includes known HBV Core interacting proteins SRPK1 and SRPK2, and p53 protein whose expression is known to be repressed due to the HBV Core interaction with the E2F1 transcription factor. Many of the newly identified possible HBV Core interacting proteins are involved in biological processes already known or are suspected to be influenced by the HBV such as translational and transporting processes or gene expression and macromolecule production. Overall, this work comprehensively characterizes the interaction landscape of the HBV Core protein in the live cells and might thus serve as a reliable start for in depth HBV-host interaction analysis. Key...
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Coat protein-RNA interaction in vivo and the biotechnological use of VLPs
Kratochvílová, Kateřina ; Moravec, Tomáš (advisor) ; Hála, Michal (referee)
The Tobacco mosaic virus (TMV) is a simple and frequently used model virus which has been studied already more over than 130 years. Due to the intensive study of this virus the details of its infectious cycle, genomic information and also the structure of the created viral particle as well as the mechanism of its creation are known today. The process of encapsidation (viral particle formation) is sufficiently described in the in vitro conditions. In the in vitro conditions the origin of assembly (OAS) was also described. The OAS was identified in the coding sequence of the gene for the movement protein (MP). The importance of replication centers (replication factories) has also been supposed. The aim of the diploma thesis was to study the specificity of the interaction of RNA and coat protein in the process of the particle assembly taking place directly inside the plants. The experiments were performed to verify the necessity of presence of OAS sequence in process of initiation of viral encapsidation. The effect of the cell compartmentation on this process has also been studied. Based on several viral systems (the Tobacco mosaic virus, the Potato virus X, the Bean yellow dwarf virus and Cowpea mosaic virus) gene constructs were created. These constructs enables to study this idea at the molecular...
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The role of capsid protein in hepatitis B virus life cycle
Eliáš, Vratislav ; Weber, Jan (advisor) ; Drda Morávková, Alena (referee)
Hepatitis B virus (HBV) can cause either an acute or a chronic infection of hepatocytes, often leading to a hepatocellular carcinoma or a liver cirrhosis. HBV encodes seven proteins in its 3.2kb genome. Two of these proteins are transcribed from the same ORF (HBcAg and HBeAg). HBeAg, as a soluble variant of the core protein, plays a crucial role in virus immunogenicity. HBcAg, apart from building viral capsid, represents a pleiotropic protein engaging in multiple viral stages. Its primary structure is divided into two domains: an assembly domain and a C-terminal domain (CTD). The latter, containing four arginine clusters, is an important life cycle regulation element. By interaction with multiple viral and cellular factors, it directs the virus through a successful replication. In this thesis, we have collected the available data about the various roles of HBcAg in viral life cycle. We believe that further investigation of this field could lead to therapeutic advances resulting in the decrease of HBV infections worldwide, subsequently to a lower lethality connected with the diseases caused by HBV. Powered by TCPDF (www.tcpdf.org)
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