Isolation and Partial Characterisation of a New Virus Causing Acute Hæmorrhagic Fever in Zaire

Johnson, Karl M.; Lange, Jens; Webb, P. A.; Murphy, Frederick A.

doi:10.1016/s0140-6736(77)92000-1

Cited by 332 publications

(175 citation statements)

References 4 publications

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“…Within the EBOV genus, ZEBOV appears to be the most pathogenic EBOV species (1,28) while, in contrast, Reston EBOV (REBOV), which is lethal in nonhuman primates, seems to be attenuated in humans, having caused seroconversion without any apparent signs of illness in the only documented human infections (4,27). When microarray analyses were performed on EBOVinfected Huh7 cells, REBOV was found to have a reduced ability compared with ZEBOV to inhibit expression of IFNinduced antiviral genes and thus evade the host antiviral response (30).…”

Section: Ebola Virus (Ebov) and Marburg Virus Comprise The Familymentioning

confidence: 99%

Ebola Virus VP24 Proteins Inhibit the Interaction of NPI-1 Subfamily Karyopherin α Proteins with Activated STAT1

Reid

Valmas

Martinez

et al. 2007

J Virol

224

249

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The Zaire ebolavirus protein VP24 was previously demonstrated to inhibit alpha/beta interferon (IFN-␣/␤)-and IFN-␥-induced nuclear accumulation of tyrosine-phosphorylated STAT1 (PY-STAT1) and to inhibit IFN-␣/␤-and IFN-␥-induced gene expression. These properties correlated with the ability of VP24 to interact with the nuclear localization signal receptor for PY-STAT1, karyopherin ␣1. Here, VP24 is demonstrated to interact not only with overexpressed but also with endogenous karyopherin ␣1. Mutational analysis demonstrated that VP24 binds within the PY-STAT1 binding region located in the C terminus of karyopherin ␣1. In addition, VP24 was found to inhibit PY-STAT1 binding to both overexpressed and endogenous karyopherin ␣1. We assessed the binding of both PY-STAT1 and the VP24 proteins from Zaire, mouse-adapted Zaire, and Reston Ebola viruses for interaction with all six members of the human karyopherin ␣ family. We found, in contrast to previous studies, that PY-STAT1 can interact not only with karyopherin ␣1 but also with karyopherins ␣5 and ␣6, which together comprise the NPI-1 subfamily of karyopherin ␣s. Similarly, all three VP24s bound and inhibited PY-STAT1 interaction with karyopherins ␣1, ␣5, and ␣6. Consistent with their ability to inhibit the karyopherin-PY-STAT1 interaction, Zaire, mouse-adapted Zaire, and Reston Ebola virus VP24s displayed similar capacities to inhibit IFN-␤-induced gene expression in human and mouse cells. These findings suggest that VP24 inhibits interaction of PY-STAT1 with karyopherins ␣1, ␣5, or ␣6 by binding within the PY-STAT1 binding region of the karyopherins and that this function is conserved among the VP24 proteins of different Ebola virus species.

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Section: Ebola Virus (Ebov) and Marburg Virus Comprise The Familymentioning

confidence: 99%

Ebola Virus VP24 Proteins Inhibit the Interaction of NPI-1 Subfamily Karyopherin α Proteins with Activated STAT1

Reid

Valmas

Martinez

et al. 2007

J Virol

224

249

View full text Add to dashboard Cite

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“…Both viruses have been isolated from patients in Africa and produce severe haemorrhagic disease with mortality as high as 9070 for EBO (Johnson et al, 1977) and 30 70 to 35 70 for MBG (Martini & Siegert, 1971). MBG virus was first isolated in 1967 from laboratory workers who had become ill after contact with tissues of monkeys imported into Europe from Uganda (Martini & Siegert, 1971), hence the alternative name 'green monkey disease'.…”

Section: Introductionmentioning

confidence: 99%

Physicochemical Properties of Marburg Virus: Evidence for Three Distinct Virus Strains and Their Relationship to Ebola Virus

Kiley

Cox

Elliott

et al. 1988

Journal of General Virology

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SUMMARYThe physicochemical and antigenic properties of three groups of Marburg (MBG) virus isolates, separated temporally and geographically, were compared to each other and to another member of the same family, Ebola (EBO) virus. Each MBG isolate contained seven virion proteins, one of which was a glycosylated surface protein.Peptide mapping of glycoproteins, nucleoproteins (NP) and viral structural protein (VP40) demonstrated extensive sequence conservation in the proteins of viruses isolated over a 13-year period, but homology was not evident in VP24. Some homology between the NPs of MBG and EBO was observed. A close antigenic relationship between MBG strains was found by radioimmunoassay but no evidence was found of antigenic cross-reactivity with EBO viruses. MBG virion proteins are produced from virus-specific monocistronic mRNA species. Five of the seven viral proteins were produced by in vitro translation of these RNAs. MBG virions contained one RNA species with an Mr of 4.2 x 106 and virions had a density of 1.14 g/ml in potassium tartrate. Virus isolates from different outbreaks had distinct TI oligonucleotide maps, but had approximately 9570 homology in base sequence. No two geographically distinct virus pairs were more closely related to each other than to a third virus isolate. MBG viruses are thus similar to EBO viruses in morphology and other physicochemical properties and are very similar to each other in RNA and protein composition. Each of the three geographically and temporally distinct MBG virus outbreaks appears to have been due to a genetically distinguishable, but antigenically closely related virus strain. In addition, these studies confirm the belief that MBG and EBO viruses are members of the new virus family, the Filoviridae.

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“…Viral hemorrhagic fevers such as that caused by the Ebola virus present a serious health threat in central and eastern Africa with fatality rates as high as 90% (1,2). The Ebola virus from the Filoviridae family uses a negative sense RNA genome encoding seven proteins to replicate in the host cell (3,4).…”

mentioning

confidence: 99%

The Ebola Virus Matrix Protein Penetrates into the Plasma Membrane

Adu-Gyamfi

Soni

Xue

et al. 2013

Journal of Biological Chemistry

123

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Background:The Ebola virus matrix protein (VP40) regulates the plasma membrane assembly and egress of the Ebola virus. Results: The plasma membrane induces membrane penetration of the VP40 C-terminal domain. Conclusion: Membrane penetration by VP40 is important for VP40 cellular localization, oligomerization, and viral budding. Significance: A better understanding of VP40-membrane interactions will help us to understand Ebola virus assembly and budding.

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Isolation and Partial Characterisation of a New Virus Causing Acute Hæmorrhagic Fever in Zaire

Cited by 332 publications

References 4 publications

Ebola Virus VP24 Proteins Inhibit the Interaction of NPI-1 Subfamily Karyopherin α Proteins with Activated STAT1

Ebola Virus VP24 Proteins Inhibit the Interaction of NPI-1 Subfamily Karyopherin α Proteins with Activated STAT1

Physicochemical Properties of Marburg Virus: Evidence for Three Distinct Virus Strains and Their Relationship to Ebola Virus

The Ebola Virus Matrix Protein Penetrates into the Plasma Membrane

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