Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q17RS7 (Gen)
 130,125 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A randomized, single-blind, controlled trial was performed at a community health center to measure the impact of computer-generated reminders mailed to patients on the rate of influenza immunization. High-risk patients were randomized to one of three groups: 1) usual care, 2) one reminder letter, offering free influenza immunization without an appointment, or 3) two sequential reminder letters, offering the same. The reminders did not significantly affect rates of influenza immunization. Analysis of the combined groups indicates that an appointment with a primary care provider remains the most reliable method of immunizing high-risk patients at this health center.
J Gen Intern Med
PMID:Computer-generated mailed reminders for influenza immunization: a clinical trial. 140 12

The schemes for preparative electrophoretic isolation and purification of major proteins from influenza virus are described. The viral envelope protein, hemagglutinin, two of its subunits, internal M and NP proteins of influenza viruses A/FPV/Rostock (H7N1), A/PR/8/34 (H1N1) and X-31 (H3N2) were obtained in preparative amounts and characterized by amino acid and N-terminus analyses.
Mol Gen Mikrobiol Virusol
PMID:[Preparative isolation of basic structural proteins of the influenza virus]. 140 60

Influenza virus particles are able to fuse with liposomes composed of negatively charged or neutral phospholipids, as shown by using fluorochrome-labelled virions and fluorescence dequenching methods. Fusion with liposomes composed of only phosphatidylcholine (PC) was dependent on the presence of cholesterol (Chol), whereas fusion with liposomes containing negatively charged phospholipids, such as phosphatidylserine (PS), or of PC and phosphatidylethanolamine (PE) occurred in the absence of Chol. Fusion of influenza virions with PC:Chol liposomes was observed at pH 5.0, but not at pH 7.4, whereas a low degree of fusion with negatively charged liposomes or those containing PE was observed at pH 7.4. In addition, non-fusogenic influenza virions or HA0 influenza virions fused with PS- or PE-containing liposomes, especially at pH 5.0. Influenza virus particles were also able to induce the release of the fluorochrome calcein from negatively charged calcein-loaded liposomes at pH 5.0, as well as at pH 7.4, but failed to do so with PC:Chol liposomes. Lysis of PC:Chol by influenza virions was dependent on the presence of virus receptors, namely gangliosides (sialoglycolipids), and was observed only at pH 5.0. The results show that fusion of influenza virions with negatively charged or PE-containing liposomes does not reflect the biological activity of the virus needed for penetration and infection of living cells. On the other hand, fusion with PC:Chol liposomes is probably due to the activity of the viral fusion protein, the haemagglutinin glycoprotein.
J Gen Virol 1992 Nov
PMID:Fusion of influenza virus particles with liposomes: requirement for cholesterol and virus receptors to allow fusion with and lysis of neutral but not of negatively charged liposomes. 143 10

The 12 nucleotide conserved sequence at the 3' end of influenza A virion RNA is sufficient to function as a promoter in vitro. By introducing point mutations in all 12 positions of this promoter in model RNA templates and studying the efficiency of RNA synthesis in vitro, we show that only three nucleotides, residues 9, 10 and 11, are crucial for activity, although other nucleotides play a significant but less important role. Additions or deletions within the promoter are tolerated, resulting in either an increase or a decrease in promoter activity, depending on the mutation introduced; in some cases premature termination is caused. Taking these observations into account, a model for RNA polymerase binding and copying of the promoter is discussed.
J Gen Virol 1992 Dec
PMID:Nucleotides 9 to 11 of the influenza A virion RNA promoter are crucial for activity in vitro. 146 51

The non-structural protein NS1 of influenza A virus exhibits two modes of RNA-binding activity. One is sequence-specific binding to minus-sense virus RNA with either a 5'- or 3'-terminal common sequence as reported previously. The other was identified as binding to dsRNA and this activity did not show sequence specificity. The affinity of binding to dsRNA was much higher than that to ssRNA. A short miniature virion RNA forming a panhandle structure by pairing between the 5'- and 3'-terminal common sequences bound NS1 with higher affinity and stability than did a dsRNA of similar sequence and length.
J Gen Virol 1992 Dec
PMID:Binding of influenza A virus NS1 protein to dsRNA in vitro. 146 70

The non-structural protein NS1, encoded by genome segment 8 of influenza A virus, was expressed in Escherichia coli from cloned cDNA and purified. The NS1 protein had a specific RNA-binding activity, binding to influenza A virus minus-sense but not plus-sense RNA synthesized in vitro from cloned DNA using phage RNA polymerase. NS1 bound preferentially to the regions of RNA containing either 5'- or 3'-terminal common sequences of the genomic RNA. Binding was inhibited by virion RNA, but not by single-stranded minus-sense cDNA and oligo DNAs having the common sequences. In addition, binding was also inhibited by 28S rRNA but not 18S rRNA prepared from MDCK cells.
J Gen Virol 1992 Jan
PMID:Specific binding of influenza A virus NS1 protein to the virus minus-sense RNA in vitro. 153 Sep 62

We investigated the possible involvement of oxidative mechanisms in the pathogenesis of influenza A/PR8/34 virus infection in mice. As a biochemical marker of oxidative stress, we determined the endogenous concentrations of the antioxidants glutathione and vitamins C and E in their reduced and oxidized forms in the lungs, liver and blood plasma of control and infected animals. Following intranasal infection with 8 to 10 LD50, influenza virus was detected in the lungs, but not in the plasma, liver or other organs. Infection resulted in a decrease in the total concentration of glutathione and vitamins C and E, whereas no relevant change in the ratio of oxidized to total concentration of antioxidants was observed. Changes in the concentration of hepatic antioxidants were significant in the early stages of the infection. The results suggest that hepatic alterations may be caused indirectly by mechanisms related to the host response to virus infection. The observed general decrease in the antioxidant buffering capacity may reduce the ability of tissues to protect against potential oxidative stress. Such stress can occur during bacterial superinfections, which are common in influenza, thereby rendering the host more susceptible to the pathogenic effects of such agents. In addition, reactive oxygen species produced in the lung may inactivate protease inhibitors, resulting in increased protease activity. Using an in vitro system consisting of alpha 1-antiprotease, trypsin and HOCl as the oxidant, we have shown that the infectivity of influenza viruses can be increased up to 10,000-fold by proteolytic cleavage of haemagglutinin, leading to activation of the fusogenic properties of this protein.
J Gen Virol 1992 Jan
PMID:Alterations in antioxidant defences in lung and liver of mice infected with influenza A virus. 153 Sep 63

Reassortant influenza A viruses bearing H1 haemagglutinin and N2 neuraminidase were isolated from humans in China between December 1988 and March 1989. As primary isolation of influenza A (H1N2) viruses from humans had not been reported previously, it was of interest to determine the genetic origin of these virus isolates. The haemagglutinins of the H1N2 viruses were antigenically and genetically related to those of H1 viruses isolated world-wide since 1986, and the neuraminidases of these viruses were antigenically and genetically related to those of recent H3N2 viruses. Partial sequencing of each gene segment of three of the H1N2 viruses revealed that all gene segments except that encoding the haemagglutinin gene were derived from virus of the H3N2 subtype. Sequence differences amongst the neuraminidase, nucleoprotein and nonstructural genes of these three H1N2 reassortant viruses as well as the isolation of reassortants in seven laboratories over a 4 month period make it unlikely that the H1N2 viruses are laboratory artefacts. The spread of these reassortant viruses to other countries has not yet been documented.
J Gen Virol 1992 Feb
PMID:Human influenza A (H1N2) viruses isolated from China. 153 94

The kinetics of cellular mRNA decay in influenza virus-infected cells have been studied by means of blot hybridization using as probes cloned cDNAs of alpha- and beta-actin, alpha- and beta-tubulin and vimentin. Both cellular mRNAs isolated from the cytoplasmic fractions as well as total cell mRNAs showed a rapid decay, with up to 50% concentration reductions at infection times at which influenza virus M1 mRNA was still not detectable. In contrast, these cellular mRNAs were stable in uninfected cells. To ascertain the possible role of mRNA degradation in the cellular protein synthesis shutoff, the kinetics of protein synthesis in infected cells were examined by two-dimensional gel electrophoresis of extracts pulse-labelled at several times after viral infection. The synthesis of the cellular proteins was reduced, showing kinetics paralleling those of mRNA decay. It is proposed that influenza virus infection induces the destabilization of mRNAs and that this mRNA degradation is, at least in part, responsible for cellular protein synthesis shutoff.
J Gen Virol 1992 Mar
PMID:Degradation of cellular mRNA during influenza virus infection: its possible role in protein synthesis shutoff. 154 20

Nucleotide sequence analysis of the gene region coding for the HA1 domain of the influenza B virus haemagglutinin was performed on seven field strains isolated during the 1989 to 1990 season and two field strains isolated in 1985 and 1988 in Finland. All isolates were antigenically and genetically related to B/Victoria/2/87 virus and distinct from B/Yamagata/16/88 virus. The three strains isolated at the beginning of the 1989 1990 season in Turku were almost identical to an American variant (B/Texas/37/88-B/Ohio/10/88) of the previous season, whereas the four strains isolated later in the 1989 to 1990 season in Helsinki formed a new group of heterogeneous viruses. The phylogenetic tree compiled suggests that the two branches had evolved from a common origin, probably in 1987.
J Gen Virol 1992 Mar
PMID:Evolution of influenza B/Victoria/2/87-like viruses: occurrence of a genetically conserved virus under conditions of low epidemic activity. 154 26


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