Morphology, Development, and Classification of the Marburg Virus

Peters, D.; Müller, G.; Slenczka, Werner

doi:10.1007/978-3-662-01593-3_10

Cited by 35 publications

(39 citation statements)

References 16 publications

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“…Virion particles appeared in multiple forms (e.g., annular, 6-shaped, U-shaped, filamentous) (Fig. 3) as described previously for propagation in other cells (30). Spikes were clearly visible on the surface of virus particles (Fig.…”

Section: Methodssupporting

confidence: 59%

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Replication of Marburg virus in human endothelial cells. A possible mechanism for the development of viral hemorrhagic disease.

Schnittler¹,

Mahner²,

Drenckhahn³

et al. 1993

J. Clin. Invest.

113

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Section: Methodssupporting

confidence: 59%

“…One type appeared as multilamellar inclusions (Fig. 4 b) similar to those found only in infected Vero cells but without showing the heavily stained strands in the periphery (30). The second type of inclusions consists ofelectron-dense filamentous material (Fig.…”

Section: Methodsmentioning

confidence: 51%

Replication of Marburg virus in human endothelial cells. A possible mechanism for the development of viral hemorrhagic disease.

Schnittler¹,

Mahner²,

Drenckhahn³

et al. 1993

J. Clin. Invest.

113

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“…MBG, the prototype filovirus, was isolated during an outbreak of haemorrhagic fever among laboratory workers in 1967 in the city of Marburg, Germany (Peters et al, 1971). The mortality rate of MBG infection was unusually high: 30 % of the cases had a fatal outcome.…”

Section: Introductionmentioning

confidence: 99%

The asialoglycoprotein receptor is a potential liver-specific receptor for Marburg virus

Becker

Spiess²,

Klenk³

1995

Journal of General Virology

160

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The liver is one of the main target organs of Marburg virus (MBG), a filovirus causing severe haemorrhagic fever with a high fatality rate in humans and non-human primates. MBG grown in certain cells does not contain neuraminic acid, but has terminal galactose on its surface glycoprotein. This observation indicated that the asialoglycoprotein receptor (ASGP-R) of hepatocytes may serve as a receptor for MBG in the liver. Binding studies revealed that the attachment of MBG to ASGP-R-expressing HepG2 cells, but not to ASGP-R-negative E6 Vero cells, has the characteristics ofligand binding to the ASGP-R: binding is dependent on calcium and is inhibited by excess asialofetuin and by anti-ASGP-R antiserum. Asialofetuin and the specific antiserum also inhibited MBG infection of HepG2 cells. In addition, it was shown that expression of ASGP-R cDNA in NIH 3T3 cells enhanced the susceptibility of these cells to MBG infection 4'5-fold. Interaction of MBG with the hepatic ASGP-R could thus explain the marked hepatotropism of the virus.

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“…Bar, 150 nm. infectious particles are released by budding at the cell surface (10,11,(16)(17)(18)(19). MBGV morphogenesis commences with the formation of intracytoplasmic blurred wavy strands which are first arranged in loose accumulations and then scattered (17).…”

mentioning

confidence: 99%

“…It has been observed that MBGV inclusions show the manifestation of nucleocapsid formation only shortly before budding, in contrast to EBOV inclusions, which as a rule contain easily discernible preformed nucleocapsids (11). Sometimes, sections of MBGV inclusions exhibit thin-walled tubule-like structures (TLS) which are organized in a hexagonal pattern (11,17). However, the exact protein composition of these TLS has not been identified.…”

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confidence: 99%

Ultrastructural Organization of Recombinant Marburg Virus Nucleoprotein: Comparison with Marburg Virus Inclusions

Kolesnikova

Mühlberger

Ryabchikova

et al. 2000

J Virol

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HeLa cells expressing the recombinant Marburg virus (MBGV) nucleoprotein (NP)have been studied by immunoelectron microscopy. It was found that MBGV NPs assembled into large aggregates which were in close association with membranes of the rough endoplasmic reticulum. Further analysis of these aggregates revealed that NPs formed tubule-like structures which were arranged in a hexagonal pattern. A similar pattern of preformed nucleocapsids was detected in intracellular inclusions induced by MBGV infection. Our data indicated that MBGV NP is able to form nucleocapsid-like structures in the absence of the authentic viral genome and other nucleocapsid-associated proteins.Marburg virus (MBGV) and Ebola virus (EBOV) make up the family of Filoviridae, which belongs to the order Mononegavirales. MBGV causes a severe hemorrhagic disease in humans and nonhuman primates (22). The recent outbreak of MBGV hemorrhagic fever in the Democratic Republic of the Congo underlines the emerging potential of this pathogen (25). MBGV is an enveloped virus with a nonsegmented negativestrand RNA genome 19.1 kb in length, which encodes seven structural proteins (5, 8). The nucleocapsid of the virion is composed of the viral RNA and four proteins, the nucleoprotein (NP), P (formerly called VP35), the viral protein VP30, and the catalytic subunit of the polymerase (L). Two putative matrix proteins, VP24 and VP40, are located between the nucleocapsid and the envelope, which is decorated with the surface protein (GP) (2,3,7,13,15,20).Viral reproduction takes place in the cytoplasm, and the FIG. 1. IEM analysis of ultrathin section of MVA-T7-infected HeLa cells expressing recombinant NP. Immunogold labeling was carried out using a monoclonal antibody directed against MBGV NP (dilution, 1:10) and a goat anti-mouse antibody conjugated with colloidal gold (bead diameter, 5 nm) (dilution, 1:50). NP aggregates appeared as two long sheets of a reticular network of electron-dense material heavily labeled with gold particles. The NP aggregates are in close association with the membrane of the rER. Bar, 150 nm.

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Morphology, Development, and Classification of the Marburg Virus

Cited by 35 publications

References 16 publications

Replication of Marburg virus in human endothelial cells. A possible mechanism for the development of viral hemorrhagic disease.

Replication of Marburg virus in human endothelial cells. A possible mechanism for the development of viral hemorrhagic disease.

The asialoglycoprotein receptor is a potential liver-specific receptor for Marburg virus

Ultrastructural Organization of Recombinant Marburg Virus Nucleoprotein: Comparison with Marburg Virus Inclusions

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