Crimean-Congo hemorrhagic fever (CCHF) is a human disease with high fatality rate. Although its pathogenesis is not elucidated yet, it is considered that cytokines play a significant role in the progression and outcome of the disease. Serum CXCL10 levels were estimated in 35 patients with acute CCHF and were correlated with the viral load, and various demographic and clinical parameters. The mean CXCL10 concentration in the patients' group was higher compared to the respective value in the control group (4421.74 pg/ml vs. 28.47 pg/ml, P < 0.05). A strong positive correlation between CXCL10 and viral load was seen (rs = 0.57, P < 0.001), while the outcome of the disease was related with the viral load (rs = 0.47, P = 0.004) and the presence of hemorrhagic manifestations (P < 0.001). The study provides an insight into the strong correlation between CXCL10 and viral load in acute CCHF cases suggesting that it plays an important role in CCHF pathogenesis.
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Objectives: 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 PDFInvestigation of Long Noncoding RNA-NRAV and Long Noncoding RNA-Lethe Expression in Crimean-Congo Hemorrhagic Fever.
J Med Virol
December 2024
Infectious Diseases and Clinical Microbiology Clinic, Sivas Medicana Hospital, Sivas, Turkey.
Crimean-Congo hemorrhagic fever (CCHF) is a zoonotic infectious disease caused by the CCHF virus, a member of the Bunyavirales order and the Orthonairoviridae family. The exact pathogenesis is not fully understood. Long noncoding RNAs (lncRNAs) are RNAs that are shown to play a role in various pathological processes of viral diseases.
View Article and Find Full Text PDFIsolation and characterization of Iwanai Valley virus, a new tick-borne nairovirus from Ixodes ovatus ticks in Hokkaido, Japan.
Arch Virol
December 2024
Department of Medical Entomology, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo, 162-8640, Japan.
Most members of the genus Orthonairovirus, represented by Crimean-Congo hemorrhagic fever virus and Nairobi sheep disease virus, are tick-borne, and some have become a public health concern in recent years. Here, we report the isolation and genetic and biological characterization of a new orthonairovirus, designated as "Iwanai Valley virus" (IWVV), from Ixodes ovatus ticks in Hokkaido, Japan. The amino acid sequence of the viral nucleoprotein (NP) was found to be 34-45% identical to those of known orthonairoviruses.
View Article and Find Full Text PDFReplicating RNA vaccine confers durable immunity against Crimean Congo hemorrhagic fever virus challenge in mice.
NPJ Vaccines
December 2024
Laboratory of Virology, Division of Intramural Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rocky Mountain Laboratories, Hamilton, MT, USA.
Spread by Hyalomma genus ticks, Crimean-Congo hemorrhagic fever virus (CCHFV) causes a severe hemorrhagic disease endemic throughout Southern and Eastern Europe, Asia, and Africa. To date, there are no widely approved vaccines for CCHFV and treatment for disease is largely supportive. Due to this lack of intervention, the WHO lists CCHFV as a high-priority pathogen.
View Article and Find Full Text PDFEngineering and structures of Crimean-Congo hemorrhagic fever virus glycoprotein complexes.
Cell
December 2024
Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA. Electronic address:
Crimean-Congo hemorrhagic fever virus (CCHFV) is a tickborne virus that can cause severe disease in humans with case fatality rates of 10%-40%. Although structures of CCHFV glycoproteins GP38 and Gc have provided insights into viral entry and defined epitopes of neutralizing and protective antibodies, the structure of glycoprotein Gn and its interactions with GP38 and Gc have remained elusive. Here, we use structure-guided protein engineering to produce a stabilized GP38-Gn-Gc heterotrimeric glycoprotein complex (GP38-Gn-Gc).
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