causes chronic hepatitis in a broad range of mammals, including primates, cats, woodchucks, and bats. Hepatitis B virus (HBV) X protein inhibits type-I interferon (IFN) signaling, thereby promoting HBV escape from the human innate immune system and establishing persistent infection. However, whether X proteins of viruses in other species display a similar inhibitory activity remains unknown. Here, we investigated the anti-IFN activity of 17 X proteins derived from various hosts. We observed conserved activity of X proteins in inhibiting TIR-domain-containing adaptor protein inducing IFN-β (TRIF)-mediated IFN-β signaling pathway through TRIF degradation. X proteins from domestic cat hepadnavirus (DCH), a novel member of , inhibited mitochondrial antiviral signaling protein (MAVS)-mediated IFNβ signaling pathway comparable with HBV X. These results indicate that inhibition of IFN signaling is conserved in X proteins.
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http://dx.doi.org/10.3390/ijms25073753 | DOI Listing |
BMC Cancer
January 2025
Centre for Medical Education, Queen's University Belfast, Belfast City Hospital, Lisburn Road, Belfast, UK.
Background: Myelofibrosis (MF) is a clonal haematopoietic disease, with median overall survival for patients with primary MF only 6.5 years. The most frequent gene mutation found in patients is JAK2, causing constitutive activation of the kinase and activation of downstream signalling.
View Article and Find Full Text PDFIn Vitro Cell Dev Biol Anim
January 2025
Department of Biology, Wilfrid Laurier University, 75 University Avenue West, Waterloo, ON, N2L 3C5, Canada.
Long dsRNA induces the expression of type I interferons (IFNs) and IFN-stimulated genes (ISGs) to establish an antiviral state. When induced prophylactically, this antiviral state can reduce the severity and mortality of viral infections. One of the limiting factors in delivering dsRNA in animal models is the lack of an effective carrier that protects the dsRNA from degradation in the extracellular space.
View Article and Find Full Text PDFVaccine
January 2025
Department of Microbiology and Immunology, College of Medicine, Seoul National University, Seoul 03080, Republic of Korea; Cancer Research Institute, College of Medicine, Seoul National University, Seoul 03080, Republic of Korea; Seoul National University Medical Research Center (SNUMRC), Seoul 03080, Republic of Korea; Department of Biomedical Sciences, College of Medicine, Seoul National University, Seoul 03080, Republic of Korea; Liver Research Institute, College of Medicine, Seoul National University, Seoul 03080, Republic of Korea; BK21 FOUR Biomedical Science Project, Seoul National University College of Medicine, Seoul 03080, Republic of Korea. Electronic address:
Tuberculosis (TB) remains a significant global health issue due to the limited efficacy of the Bacillus Calmette-Guérin (BCG) vaccine, highlighting the need for the development of an improved TB vaccine. In this study, we created a novel TB subunit vaccine consisting of TB-secreted chorismate mutase (TBCM) (Rv1885c) and a hepatitis B virus (HBV)-derived peptide (Poly6), which elicits Type I interferon responses, both with and without an alum adjuvant. We evaluated the immunogenicity, protective efficacy, and therapeutic efficacy of this vaccine candidate in an in vivo mouse model.
View Article and Find Full Text PDFNat Commun
January 2025
Ruminant Diseases Research Center, College of Life Sciences, Shandong Normal University, Jinan, Shandong, China.
Phenazine biosynthesis-like domain-containing protein (PBLD) and Cedrelone have been identified as tumor suppressors. However, their roles in virus infection remain unclear. Here, we demonstrate that PBLD upregulates the type I interferon (IFN-I) response through activating NF-kappaB (NF-κB) signaling pathway to resist viral infection in cells and mice.
View Article and Find Full Text PDFClin Transl Med
January 2025
Department of Neurology, The Third Affiliated Hospital of Sun Yat-sen University, Guangzhou, China.
Background: Anti-N-methyl-D-aspartate receptor encephalitis (anti-NMDARE) is a prevalent type of autoimmune encephalitis caused by antibodies targeting the NMDAR's GluN1 subunit. While significant progress has been made in elucidating the pathophysiology of autoimmune diseases, the immunological mechanisms underlying anti-NMDARE remain elusive. This study aimed to characterize immune cell interactions and dysregulation in anti-NMDARE by leveraging single-cell multi-omics sequencing technologies.
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