Rift Valley fever virus (RVFV) is a zoonotic pathogen with pandemic potential. RVFV entry is mediated by the viral glycoprotein (Gn), but host entry factors remain poorly defined. Our genome-wide CRISPR screen identified low-density lipoprotein receptor-related protein 1 (mouse Lrp1/human LRP1), heat shock protein (Grp94), and receptor-associated protein (RAP) as critical host factors for RVFV infection. RVFV Gn directly binds to specific Lrp1 clusters and is glycosylation independent. Exogenous addition of murine RAP domain 3 (mRAP) and anti-Lrp1 antibodies neutralizes RVFV infection in taxonomically diverse cell lines. Mice treated with mRAP and infected with pathogenic RVFV are protected from disease and death. A mutant mRAPD3 that binds Lrp1 weakly failed to protect from RVFV infection. Together, these data support Lrp1 as a host entry factor for RVFV infection and define a new target to limit RVFV infections.
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http://dx.doi.org/10.1016/j.cell.2021.09.001 | DOI Listing |
Front Vet Sci
December 2024
Institute of Virology, Charité-Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlinand Humboldt-Universität zu Berlin, Berlin, Germany.
Introduction: Brucellosis and Rift Valley fever (RVF) are neglected zoonotic diseases (NZD) that threaten public health, animal health, and production in resource-limited countries including Namibia.
Methods: The objective of this cross-sectional study was to determine spp. and RVFV seroprevalence in cattle at the wildlife-livestock interface in the Kabbe South constituency (Zambezi region) of Namibia.
Virol J
December 2024
Animal Production and Health Laboratory, Joint FAO/IAEA Centre of Nuclear Techniques in Food and Agriculture, Department of Nuclear Sciences and Applications, International Atomic Energy Agency, Vienna, Austria.
The three members of the genus capripoxvirus (CaPV), lumpy skin disease virus (LSDV), sheeppox virus (SPPV), and goatpox virus (GTPV) have common hosts and areas of overlapping geographical distribution with Rift Valley fever virus (RVFV). Hence, to ensure more cost-effective disease surveillance we developed and evaluated a Luminex assay for the simultaneous detection of antibodies against CaPV and RVFV in domestic ruminants. In cattle, the assay had a sensitivity (Se) of 98.
View Article and Find Full Text PDFObjectives: Arboviruses pose a significant global health challenge. This study investigated the seroprevalence of major human arboviral infections, including yellow fever (YFV), dengue (DENV), Crimean-Congo hemorrhagic fever (CCHF), Rift Valley fever (RVF), West Nile virus (WNV), and chikungunya (CHIK), in Darfur region from September to December 2018. ELISA-IgM was used to detect antibodies.
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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