Rift Valley fever (RVF) is an important zoonotic viral disease affecting several species of domestic and wild ruminants, causing major economic losses and dozens of human deaths in various geographical areas of Africa, where it is endemic. Although it is not present in Europe, there is a risk of its introduction and spread linked to globalisation and climate change. At present, the only measure that could help to prevent the disease is vaccination of flocks in areas at risk of RVF. Available live attenuated vaccines are an effective means of controlling the disease, but their use is often questioned due to residual virulence, particularly in susceptible hosts such as pregnant sheep. On the other hand, no vaccine is currently licensed for use in humans. The development of safe and effective vaccines is therefore a major area of research. In previous studies, we selected under selective mutagenic pressure a highly attenuated RVFV 56/74 virus variant called 40Fp8. This virus showed an extremely attenuated phenotype in both wild-type and immunodeficient A129 (IFNARKO) mice, yet was still able to induce protective immunity after a single inoculation, thus supporting its use as a safe, live attenuated vaccine. To further investigate its safety, in this work we have analysed the attenuation level of 40Fp8 in immunosuppressed mice (A129) when administered by the intranasal route, and compared it with other attenuated RVF viruses that are the basis of vaccines in use or in development. Our results show that 40Fp8 has a much higher attenuated level than these other viruses and confirm its potential as a candidate for safe RVF vaccine development.
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http://dx.doi.org/10.1371/journal.pntd.0012011 | DOI Listing |
Introduction: Rift Valley Fever (RVF) has caused outbreaks in Africa, impacting human health and animal trade. Recently, sporadic detections among humans and animals in East Africa have replaced large-scale outbreaks. We assessed RVF knowledge levels in East and Central Africa across countries with different epidemiological profiles.
View Article and Find Full Text PDFMethods Mol Biol
December 2024
Department of Pathology, The Sealy Institute for Vaccine Sciences, The Center for Biodefense and Emerging Infectious Diseases, The University of Texas Medical Branch at Galveston, Galveston, TX, USA.
Oropouche fever, a mosquito- or midge-borne emerging zoonotic disease endemic to South and Central America, manifests as a dengue-like acute febrile illness with occasional occurrences of meningitis or meningoencephalitis. The causative agent, Oropouche virus (OROV), belongs to the genus Orthobunyavirus within the family Peribunyaviridae. Its tripartite negative-sense RNA genome comprises small (S), medium (M), and large (L) segments, encoding structural N, Gn/Gc, and L proteins, respectively.
View Article and Find Full Text PDFMethods Mol Biol
December 2024
Wageningen Bioveterinary Research (WBVR), RA, Lelystad, The Netherlands.
High-density suspension cultures of insect cells offer a scalable and serum-free system for the expression of recombinant proteins. Rift Valley fever virus (RVFV), an arthropod-borne virus spread by mosquitoes, contains two envelop glycoproteins Gn and Gc. These glycoproteins are crucial for eliciting neutralizing antibodies that can offer protection against RVFV infection.
View Article and Find Full Text PDFMethods Mol Biol
December 2024
Faculty of Veterinary Medicine, Department of Pathology, Fundamental and Applied Research for Animals and Health (FARAH), University of Liège, Liège, Belgium.
The recombinant expression and purification of viral proteins are a key component in the study of the immune response of viruses, as well as the creation of diagnostic techniques for the detection of viruses. For structurally simple proteins, one commonly used technique is the production of recombinant proteins in bacterial expression systems, which enable the large-scale synthesis and purification of recombinant viral proteins. In this technique, the cDNA encoding for a viral protein is cloned into a bacterial expression vector (with an appropriate purification tag), produced in a modified bacterial culture, and optimized for maximum protein production in a minimal amount of time.
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