Marburg Virus Glycoprotein

Marburg virus MARV and Ebola virus EBOV constitute the family Filoviridae of enveloped viruses filoviruses that cause severe hemorrhagic fever. Two marburgviruses Marburg virus MARV and Ravn virus RAVV are highly lethal human pathogens.

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Compared to Ebola GP EGP Marburg GP MGP is less well characterized in viral entry.

Marburg virus glycoprotein. Volchkov et al 1998b. Marburgviruses are notable for encoding only a single glycoprotein GP 12 from their GP genes Feldmann et al 1992. We aimed to assess the safety and immunogenicity of two investigational DNA vaccines one EBO vaccine encoding Ebola virus Zaire and Sudan glycoproteins and one MAR encoding Marburg virus glycoprotein.

GP is a type I transmembrane protein that is assembled as a homotrimer and constitutes the spikes on virions Sanchez et al 1998. Under the current model the protein has at least 3 conformational states. Fusion of virus membrane with the vesicle membrane.

Unedited GP mRNA yields the nonstructural glycoprotein sGP which is secreted extensively from infected cells. Pre-fusion native state pre-hairpin intermediate state. Compared to Ebola GP EGP Marburg GP MGP is less well characterized in viral entry.

Marburg virus disease was initially detected in 1967 after simultaneous outbreaks in Marburg and Frankfurt in Germany. Ribonucleocapsid is released into the cytoplasm. One major determinant of host tropism for filoviruses is viral glycoprotein GP which is involved in receptor binding and viral entry.

The key player to assemble the filamentous Marburg virus particles is the matrix protein VP40 which orchestrates recruitment of nucleocapsid complexes and the viral glycoprotein GP to the budding. Here we report that co-expression of MARV glycoprotein and matrix protein VP40 in mammalian cells leads to spontaneous budding of filamentous particles strikingly similar to wild-type MARV. Synthesis of GP involves proteolytic processing by the proprotein convertase furin at a polybasic cleavage site.

Marburg virus is a hemorrhagic fever virus of the Filoviridae family of viruses and a member of the species Marburg marburgvirus genus MarburgvirusMarburg virus MARV causes Marburg virus disease in humans and other primates a form of viral hemorrhagic fever. Ebola virus and Marburg virus cause serious disease outbreaks with high case fatality rates. To better define the genetic variation within the species VP35 and glycoprotein GP genes of representative human isolates from four known episodes of Marburg virus hemorrhagic fever were analyzed.

Expression of the spike glycoprotein of Ebola virus but not of Marburg virus requires transcriptional editing. Virions are filamentous in shape but particles can also be branched circular U-shaped or 6shaped. One major determinant of host tropism for filoviruses is viral glycoprotein GP which is involved in receptor binding and viral entry.

Abstract Marburg virus the prototype of the familyFiloviridaediffers genetically serologically and morphologically from Ebola viruses. And in Belgrade Serbia. Marburg virus was propagated in E6 cells a cloned cell line of Vero cells in the presence of 6- 3 Hglucosamine Radiolabelled viral glycoprotein was digested with trypsin and oligosaccharides were liberated by sequential treatment with endo-β- N -acetylglucosaminidase H peptide-N 4 - N -acetyl-β-glucosaminylasparagine amidase F and O.

Marburg virus is the causative agent of Marburg virus disease MVD a disease with a case fatality ratio of up to 88 but can be much lower with good patient care. The virus is considered to be extremely dangerous. In this study we generated MARV virus-like particles VLPs by co-expressing the glycoprotein GP and matrix protein VP40 using the baculovirus expression system.

Processing of the transmembrane glycoprotein GP of Marburg virus involved the conversion of an endo H-sensitive ER-specific form into an endo H-resistant Golgi-specific precursor that was cleaved into GP 1 and GP 2. The World Health Organization WHO rates it as a Risk Group 4 Pathogen. GP2 acts as a class I viral fusion protein.

In this study using a human immunodeficiency virus. Attachment to host receptors through GP glycoprotein mediates is endocytosed into vesicles in the host cell by apoptotic mimicry. MARV VLPs and three adjuvants Poria cocos polysaccharide PCP-II polyIC and aluminium hydroxide were evaluated after intramuscular vaccination in mice.

N-Heterocyclic borneol derivatives as inhibitors of Marburg virus glycoprotein-mediated VSIV pseudotype entry A. Commun 2017 8 2233 DOI. Marburg virus MARV the causative agent of a severe hemorrhagic fever has a characteristic filamentous morphology.

Infection by MARV requires fusion between the host cell and viral membranes a process that is mediated by the two subunits of the envelope glycoprotein GP1 surface subunit and GP2 transmembrane subunit. Sequential transcription viral mRNAs are capped and polyadenylated by polymerase stuttering in the cytoplasm.

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