Ubiquitin Specific Protease 7 Case Study

Since we have already known the amino sequence of the protein in previous step, we can narrow down the targeting ubiquitin ligase based on existing research data such as papers, NCBI data.

A protease inhibitor is therefore a drug used to interfere with the key stage of viral replication and used to stop this fatal process.

Researchers at George Washington University have been working on a vaccine to prevent infection from the hookworm parasite for years and sought out volunteers that would let these parasitic worms burrow into their skin. In order to effectively study the hookworm, the researchers needed to find healthy volunteers that would allow the hookworm parasites to infiltrate their bodies and live in there for several months and also diseased participants to compare the data that they would collect. However, people weren’t interested in doing the clinical trial when they found out they would have parasites sucking on their blood through their intestines. After searching for months, the GW team found a small group of volunteers to take on the task

Due to the HEPN domains property of dimerizing, sacsin’s interaction with JIP3 cannot be confirmed to act through though HEPN. Performing a pulldown assay with a mutated hepen construct which retains the property of binding but is unable to dimerize would indicate that HEPN interacts with JIP3. A mutated construct of HEPN construct called ARSACS Asn-4549 mutation exists, which disrupts the HEPN dimer interface due to the replacement of an asparagine with aspartic acid in the α4-α5 loop near the edge of the HEPN dimer interface. However, this construct destabilizes HEPN folding through the introduction of a charge at the dimer interface and loss of two polar contacts. Furthermore, the expression of this HEPN

In this study, they are targeting two functions for NS1A, the version of the NS1 protein associated with influenza A virus. The two functions being studied are involved in viral replication, which are a double- stranded RNA- binding and binding to an effector domain. The binding properties of NS1B, the version of NS1 protein that is associated with influenza B virus, are also under study. Because of these functions, the binding sites of both, NS1A and NS1B will be targeted for new drug development; ultimately, to create a more effective antiviral to treat the influenza virus. Along with Dr. Krug’s study, other researchers are also studying the connection of NS1 and Influenza A

The synthesis of the viral glycoproteins HA & NA starts in the cytoplasm and later these growing polypeptide chains are transported to the endoplasmic reticulum where the proteins are modified and assembled into trimers and tetramers ( Samji T.,2009).These proteins are then transported through the Golgi apparatus and the trans-Golgi network to the plasma membrane of the cell where they inserted finally. The synthesis and folding of viral core proteins occur entirely in the cytoplasm. NP and the RNA polymerase components interact with newly synthesized viral RNA to form RNPs. The M1 protein forms interaction with the C-terminal domains of HA and NA protein on the cell plasma membrane. The newly formed RNPs interact with the M1 protein. This interaction also stops re-entry of RNPs inside the nucleus of the cell. After attachment of RNPs to M1protein where it act as a bridge on the inner half of the cell plasma membranes, in a process of budding, the new virus particles are assembled . The progeny virions bud off from the host cell. (Shi etal.,2014).As soon as budding takes place, the new virions are still attached to the cell surface through interaction of the HA with sialic acid moieties on cellular glycoproteins or glycolipids. The

The E6 and E7 proteins play and important rule in oncogenic property of human papillomavirus that can cause anogenital cancers as their high risk factor and warts as their low risk factor. E6 AND E7 proteins promote cell growth by inactivating the tumor suppressor proteins P53 and PRb (5).

The long filaments are 80 nm in diameter and either 800–1000 nanometers long. RNA is only 1% of the mass of the virus. The large virus structure is composed of three compartments the nucleocapsid, the matrix space and the envelope. The central core of each filovirus virion consists of the single RNA genomic molecule and its adherent nucleoproteins NP and VP30 (the nucleocapsid). They are linked by matrix proteins VP24 and VP40 to the inner surface of the lipid bilayer of the viral envelope, which is derived from the host cell. Trimeric spikes of the surface envelope glycoprotein are anchored in the bilayer. Two other proteins, VP35 and large protein (RNA-dependent RNA polymerase), are also present within the virion. The surface GP is coded by the GP gene, and is expressed in two molecular forms (GP1 and GP2) that are generated by an RNA editing mechanism; it has important roles in virus infection and pathogenesis, and its expression is tightly regulated during virus replication. It has been recently demonstrated that the level of GP1 and 2 expressions regulates the virus production and

The proteins are E1-E7 and L1-L2. E stands for early, while L stands for late. E6 and E7 are the two most studied proteins. They have important roles as p53 tumor suppressor and inhibitor of differentiation, respectively(3). Although both E6 and E7 have garnered much attention as potential therapeutic targets, E5 is largely unrecognized.

Abstract- Human bocavirus is a single-stranded DNA virus. HBoV was discovered in 2005 within a nasopharyngeal sample. HBoV belongs to the Parvoviridae family, these group members contain four proteins. HBoV, in particular, contains two nonstructural proteins which are called NS1 and NP1. HBoV also contains two overlapping capsid proteins which called VP1 and VP2 (Z. Zhou et al., 2014). The non-structural NS1 had been identified as main proteins that are responsible for genome transcription, replication, and packaging in the viral cell cycle. Patients with HBoV infection express various signs and symptoms such as rhinitis, pharyngitis, cough, dyspnea, wheezing, pneumonia, fever, nausea, vomiting, and diarrhea (Jartti et al., 2012). HBoV can

The tumor suppressor gene p53 is any variant of a protein that is prearranged by homologous genes in a variety of organisms. The tumor suppressor gene is essential in multicellular organisms due to its function of preventing cancer development, therefore giving its identity of being a “tumor suppressor”. In the year 1979, the protein p53 was discovered bound to the T antigen found in the simian virus (SV40). Because it was found exceptionally in its mutant form, it was first thought of being an oncogene; it was not until ten years later that the protein was determined to be a crucial aspect in tumor suppression.

An oncolytic virus (OV) is a virus that preferentially infects and kills cancer cells. OVs posses the ability to selectively infect and replicate in cancer and associated endothelial cells and kill these cells in cancerous tissues while leaving normal tissues unharmed [1]. As the infected cancer cells are destroyed by lysis, they release new infectious virus particles to help destroy other cancer cells or the remaining tumor. The viruses achieve this by a number of mechanisms, including direct lysis, apoptosis, expression of toxic particles, shutdown of protein synthesis, as well as the induction of anti-tumoral immunity.

Although many RBPs recognize RNA in a sequence specific manner, sequence information alone is not sufficient to reliably predict ICP27 binding sites. In the infected cell, other RBPs will cooperate and compete when binding to viral transcipts; therefore it is critical to study ICP27-RNA interactions within the cellular environment. The iCLIP-seq experiments will provide an in vivo, transcriptome-wide map of ICP27-RNA binding sites during lytic HSV-1 infection. Importantly, the high resolution of iCLIP-seq should allow us to identify a consensus recognition element from which oligonucleotides will be generated for use in Specific Aim 2. In the case that the standard iCLIP conditions

In the absence of a cure for HIV Type 1 (HIV-1) pathogenesis, highly active antiretroviral therapy (HAART) are designed to suppress viral replication and maintain it at low to undetectable levels (Prabu-Jeyabalan et al, 2002). Due to their high intrinsic antiviral activity, the introduction of HIV-1 protease inhibitors (PIs) have led to a dramatic reduction in morbidity and mortality rates of HIV-1 infected patients (Codoner et al, 2017). HIV-1 protease inhibitors are peptidomimetics, or substrate or transition state analogs that mimic natural peptides or proteins and retain the ability to interact with the original protein’s biological target, that competitively targets the hydrophobic P2-P2’ domain in the active site (Prabu-Jeyabalan et

Epstein-Barr-virus (EBV) is a member of the gamma herpesvirus family that establishes a persistent infection in approximately 90% of the world’s population. In immunocompromised individuals, EBV infection can contribute to cancer development like nasopharyngeal carcinoma, Burkitt lymphoma and Hodgkin’s disease. The latent membrane protein 1 (LMP1) is expressed in most EBV-associated cancers and it is well established that LMP1 is a major viral oncogene. Expression of LMP1 alone is sufficient to transform cells and recombinant EBV lacking LMP1 is incapable of immortalizing B-cells in vitro. Moreover, transgenic mice expressing LMP1 behind a B-cell specific promoter develop lymphomas.