Ebola virus (of the Filoviridae family) was first identified in 1976 in the Democratic Republic of Congo (ex- Zaire). It has been the source of several lethal epidemics in central Africa. Four subtypes exist, three of which rage on the African continent. The zaire subtype, the most dangerous for humans, was responsible for eight epidemics which have hit Gabon and the Republic of Congo since 1995. Infection by this subtype in humans is expressed by a violent haemorrhagic fever which in 80 % of cases kills the victim in a few days. There has been a succession of 14 epidemics of Ebola in Africa since 1976. Ten of which were caused by the zaire sub-type, generating 1850 cases resulting in 1300 deaths.
Viral transmission to humans occurs by way of direct contact with infected primate carcasses (1). However, although they are the source of human infection, these animals are not the reservoir for the virus. The large primates develop the disease and die only days after themselves being infected, following contamination events provoked by contact with the reservoir. Numerous investigations, conducted since 1976 and aiming to identify this reservoir, have been unsuccessful. Eric Leroy of the IRD in Gabon and his co-workers from the CIRMF have now identified some tropical bat species as a potential Ebola virus reservoir, the fruit of studies they undertook between 2001 and 2003 in the border region between Gabon and the Republic of Congo. They publish their findings today.
The human epidemics that have flared up since 2001 were linked to multiple viral outbreaks in several animal species including chimpanzees, gorillas and duiker. During these epidemic episodes, the researchers captured about 1000 small vertebrates in good health (rodents, shrews, bats, birds and squirrels) from the vicinity of carcasses of infected primates. They performed a range of analyses: a search for specific Ebola virus antibodies in the serum, and for viral genome in certain organs; isolation of the virus on sensitive cell lines; immunohistochemistry of organ sections.
Beatrice LE BRUN | alfa
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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