A5050987285- Influenza Virus Research Studies
- RNA Research and Splicing
- interferon and immune responses
- RNA and protein synthesis mechanisms
- Respiratory viral infections research
- Genomics and Chromatin Dynamics
- RNA modifications and cancer
- Virus-based gene therapy research
- Viral Infections and Immunology Research
- Viral gastroenteritis research and epidemiology
- Virology and Viral Diseases
- DNA Repair Mechanisms
- DNA and Nucleic Acid Chemistry
- RNA Interference and Gene Delivery
- Epigenetics and DNA Methylation
- CRISPR and Genetic Engineering
- Immune Response and Inflammation
- Cancer-related gene regulation
- Bacterial Genetics and Biotechnology
- Cytokine Signaling Pathways and Interactions
- Viral Infectious Diseases and Gene Expression in Insects
- Animal Virus Infections Studies
- Cancer-related molecular mechanisms research
- Inflammasome and immune disorders
- HIV Research and Treatment
University of Tsukuba
2016-2025
Tsukuba University of Technology
2021
Biology of Infection
2021
University of Health Science
2021
Marmara University
2021
Pharmaceuticals and Medical Devices Agency
2018
Faculty (United Kingdom)
2014-2018
Ankara University
2016
Yokohama City University
2012
Tokyo Institute of Technology
1991-2010
Retinoic acid inducible gene I (RIG-I)-like receptors (RLRs) function as cytoplasmic sensors for viral RNA to initiate antiviral responses including type interferon (IFN) production. It has been unclear how RIG-I encounters and senses RNA. To address this issue, we examined intracellular localization of in response infection using newly generated anti-RIG-I antibody. Immunohistochemical analysis revealed that RLRs localized virus-induced granules containing stress granule (SG) markers...
Transcription and replication of the influenza virus RNA genome occur in nuclei infected cells through viral RNA-dependent polymerase consisting PB1, PB2, PA. We previously identified a host factor designated RAF-1 (RNA activating 1) that stimulates synthesis. is found to be identical Hsp90. Here, we examined intracellular localization Hsp90 subunits their molecular interaction. was interact with PB2 it relocalized nucleus upon infection. nuclear transport occurs expressing alone. The...
Efficient transcription and replication of the influenza virus genome are dependent upon host-derived factors. Using an <i>in vitro</i> RNA synthesis system, we have purified identified Hsp90 as one host factors that stimulate viral polymerase activity. interacted with PB2 subunit through amino-terminal chaperone domain middle region containing a highly acidic domain. The was also responsible for its stimulatory We found portion is re-localized to cell nucleus after infection. A fragment...
Measles virus (MV), a member of the family Paramyxoviridae, encodes C and V non‐structural proteins. To clarify functions MV proteins, HeLa cell lines constitutively expressing or protein were established. We found that expression inhibited interferon (IFN)‐α/β signaling but not IFN‐γ signaling. had no inhibitory effect on IFN in our experimental condition. Degradation selective signal transducers activators transcription (STAT) proteins was observed cells protein. In contrast, tyrosine...
It is well established that the transcription rate of rRNA gene closely associated with profound alterations in cell growth rate. Regulation likely to be dependent on dynamic conversion chromatin structure. Previously, we identified B23/nucleophosmin, a multifunctional nucleolar phosphoprotein, as component template activating factor III remodels chromatin-like structure adenovirus genome complexed viral basic proteins. has also been shown B23 histone chaperone activity. Here, examined...
Ribonucleoprotein (RNP) cores of influenza virus A/PR/8/34 were dissociated into RNA polymerase (PB1-PB2-PA complex)-associated genome and nuclear protein (NP) fractions by CsCl centrifugation. The polymerase-RNA complexes capable catalyzing the endonucleolytic cleavage capped RNA, initiation primer-dependent synthesis, synthesis small-sized but unable to synthesize template-sized RNA. By adding NP complexes, RNP (RNA polymerase-RNA-NP) reconstituted; they synthesized tem plate-sized...
Influenza A virus RNA genome exists as eight-segmented ribonucleoprotein complexes containing viral polymerase and nucleoprotein (vRNPs). Packaging of vRNPs budding take place at the apical plasma membrane (APM). However, little is known about molecular mechanisms transport newly synthesized vRNP. Transfection fluorescent-labeled antibody subsequent live cell imaging revealed that punctate vRNP signals moved along microtubules rapidly but intermittently in both directions, suggestive vesicle...
ABSTRACT Respiratory epithelial cell death by influenza virus infection is responsible for the induction of inflammatory responses, but exact mechanism not understood. Here we showed that induces apoptosis and pyroptosis in normal or precancerous human bronchial cells. Apoptosis was induced only malignant tumor cells infected with virus. In respiratory (PL16T), number apoptotic increased at early phases infection, pyroptotic were observed late infection. These findings suggest pathway...
Inflammasomes are cytosolic multimolecular protein complexes that stimulate the activation of caspase-1 and release mature forms interleukin-1β (IL-1β) IL-18. We previously demonstrated influenza A virus M2 stimulates IL-1β secretion following nucleotide-binding oligomerization domain (NOD)-like receptor family pyrin domain-containing 3 (NLRP3) inflammasome. The nonstructural 1 (NS1) inhibits secretion. However, precise mechanism by which NS1 remains unknown. Here, we showed J774A.1...
Nucleophosmin/B23 is a nucleolar phosphoprotein. It has been shown that B23 binds to nucleic acids, digests RNA, and localized in granular components from which preribosomal particles are transported cytoplasm. The intracellular localization of significantly changed during the cell cycle. Here, we have examined cellular proteins effect mitotic phosphorylation B23.1 on its RNA binding activity. Two splicing variants proteins, termed B23.2, were complexed both vivo vitro. activity was impaired...
ABSTRACT Previous biochemical data identified a host cell fraction, designated RAF-2, which stimulated influenza virus RNA synthesis. A 48-kDa polypeptide (RAF-2p48), cellular splicing factor belonging to the DEAD-box family of RNA-dependent ATPases previously BAT1 (also UAP56), has now been as essential for RAF-2 stimulatory activity. Additionally, RAF-2p48 was independently an nucleoprotein (NP)-interacting protein, NPI-5, in yeast two-hybrid screen mammalian cDNA library. In vitro,...
Influenza is an infectious disease caused by the influenza virus, and each year many people suffer from this disease. Hemagglutinin (HA) in membrane of type A viruses recognizes sialylglycoconjugate receptors on host cell surface at initial step infection process; consequently, HA inhibitors are considered potential candidates for antiviral drugs. We identified peptides that bind to receptor-binding sites through a multiple serial selection phage-displayed random peptide libraries. Using H1...
Replication of influenza viral genomic RNA (vRNA) is catalyzed by RNA-dependent polymerase (vRdRP). Complementary (cRNA) first copied from vRNA, and progeny vRNAs are then amplified the cRNA. Although vRdRP minimal requirements, efficient cell-free replication could not be reproduced using only these factors. Using a biochemical complementation assay system, we found novel activity in nuclear extracts uninfected cells, designated IREF-2, that allows robust unprimed vRNA synthesis cRNA...
Influenza virus M1 protein has been shown to inhibit the transcription catalyzed by viral ribonucleoprotein complexes isolated from virions. Here, this inhibition mechanism was studied with recombinant purified Escherichia coli expressing it cDNA. RNA mobility shift assays indicated that both soluble and aggregate forms of M1, which were separated glycerol density gradient, bound RNA. Once an M1-RNA complex formed, free cooperatively rather than In addition, capable binding preformed...
Reconstitution of influenza virus nucleoprotein (NP)-RNA complexes was performed with segment 8 RNA, which synthesized in vitro from cDNA, and NP purified virions. Under optimum conditions established using a filter binding assay gel retardation assay, found to bind any RNA longer than 15 nucleotides. NP-RNA formed at 30 degrees C are more resistant high concentrations NaCl those 0 C. Treatment N-ethylmaleimide gave no effect on its activity, whereas treatment alkaline phosphatase enhanced...