ribonuclease/hitasótt

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Glycoprotein E2 of classical swine fever virus: expression in insect cells and identification as a ribonuclease.

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Two regions of amino acids homologous to the ribonuclease catalysis domain of the fungal RNases T2 of Aspergillus oryzae and Rh of Rhizopus niveus and the plant S-glycoproteins of Nicotiana alata are perfectly conserved in the amino acid sequence of the envelope glycoprotein E2 of classical swine

Lipopolysaccharide-induced expression of multiple alternatively spliced MEFV transcripts in human synovial fibroblasts: a prominent splice isoform lacks the C-terminal domain that is highly mutated in familial Mediterranean fever.

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OBJECTIVE To investigate the expression of the familial Mediterranean fever (FMF) gene (MEFV) in human synovial fibroblasts. METHODS MEFV messenger RNA in synovial fibroblasts, chondrocytes, and peripheral blood leukocytes (PBLs) was analyzed by semiquantitative and real-time polymerase chain

Tonsillar antimicrobial peptide (AMP) expression profiles of periodic fever, aphthous stomatitis, pharyngitis, cervical adenitis (PFAPA) patients.

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BACKGROUND PFAPA (periodic fever, aphthous stomatitis, pharyngitis and cervical adenitis) is the most frequent non-infectious cause of high fever observed among the European child population. While its cause is still not yet fully identified, PFAPA patients were previously shown to have altered

Secreted expression of the classical swine fever virus glycoprotein E(rns) in yeast and application to a sandwich blocking ELISA.

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E(rns) is an envelope glycoprotein of classical swine fever virus (CSFV) with RNase activity. The purpose of this study was to produce an active E(rns) for further applications using the yeast secreted expression system. The E(rns) gene was cloned into the expression vector pGAPZalphaC which was

Classical swine fever virus Erns glycoprotein antagonizes induction of interferon-beta by double-stranded RNA.

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Classical swine fever virus (CSFV) is capable of counteracting innate cellular antiviral responses by inhibiting type I interferon (IFN)-alpha/beta induction. A function associated with CSFV N(pro), with respect to the inhibition of IFN-beta production, has been clearly elucidated. In this study, we

Identification of a structural glycoprotein of an RNA virus as a ribonuclease.

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One of the three structural glycoproteins of classical swine fever virus (CSFV) is E0, a disulfide-bonded homodimer that induces virus-neutralizing antibodies and occurs in a virion-bound as well as a secreted form. E0 was shown to be similar to a family of fungal and plant ribonucleases. Purified

Polyadenylic acid sequences in the genomic RNA of the togavirus of simian hemorrhagic fever.

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Since serologic studies have failed to relate the togavirus simian hemorrhagic fever (SHF) virus to any currently accepted genus within the Togaviridae family, the presence of polyadenylic acid [poly(A)] in the genomic RNA was analyzed in view of the different content reported for the two major

Serum ribonuclease elevations and pancreatic necrosis in acute pancreatitis.

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Pancreatic necrosis is a principal determinant of the severity, duration, and infectious complications of acute pancreatitis. There has been no objective index for pancreatic necrosis, and its recognition has necessarily rested upon nonspecific clinical signs, including later deterioration or

Mild hyperthermia predisposes tumor cells to undergo apoptosis upon treatment with onconase.

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Onconase (ONC), (ranpirnase) a cytotoxic ribonuclease isolated from amphibian oocytes and early embryos targeting tumor cells in vitro and in vivo, is currently in a confirmatory Phase IIIb clinical trial for unresectable malignant mesothelioma where it demonstrates antitumor activity with

Studies on the pathogenesis of fever. II. Characterization of fever-producing substances from polymorphonuclear leukocytes and from the fluid of sterile exudates.

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Further studies on fever production by injection of leukocyte extracts or cell-free supernatant fluids from peritoneal exudates in rabbits are reported. Granulocytes collected from peripheral blood or from pleural exudates contain a heat-labile pyrogenic substance. The material in extracts of

Structure of the Rift Valley fever virus nucleocapsid protein reveals another architecture for RNA encapsidation.

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Rift Valley fever virus (RVFV) is a negative-sense RNA virus (genus Phlebovirus, family Bunyaviridae) that infects livestock and humans and is endemic to sub-Saharan Africa. Like all negative-sense viruses, the segmented RNA genome of RVFV is encapsidated by a nucleocapsid protein (N). The 1.93-A

Two cellular proteins that interact with a stem loop in the simian hemorrhagic fever virus 3'(+)NCR RNA.

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Both full-length and subgenomic negative-strand RNAs are initiated at the 3' terminus of the positive-strand genomic RNA of the arterivirus, simian hemorrhagic fever virus (SHFV). The SHFV 3'(+) non-coding region (NCR) is 76 nts in length and forms a stem loop (SL) structure that was confirmed by

An RNA-hydrolyzing recombinant antibody exhibits an antiviral activity against classical swine fever virus.

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Some proteins with ribonuclease (RNase) activity have been shown to suppress viral replication. A well-characterized recombinant antibody, 3D8 single-chain variable fragment (3D8 scFv), has RNA-hydrolyzing and cell-penetrating activities. Here, we investigated antiviral activity of 3D8 scFv against

Efficient sensing of infected cells in absence of virus particles by plasmacytoid dendritic cells is blocked by the viral ribonuclease E(rns.).

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Plasmacytoid dendritic cells (pDC) have been shown to efficiently sense HCV- or HIV-infected cells, using a virion-free pathway. Here, we demonstrate for classical swine fever virus, a member of the Flaviviridae, that this process is much more efficient in terms of interferon-alpha induction when

Dimerization of glycoprotein E(rns) of classical swine fever virus is not essential for viral replication and infection.

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The pestivirus glycoprotein E(rns), a ribonuclease, is expressed on the surface of virions and in infected cells as a disulfide-linked homodimer. E(rns) is involved in the infection process and its RNase activity is probably involved in viral replication and pathogenesis. The most C-terminal

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