Search PubMed⌕ Search

Biomedical subjects

S Nakada

Publications and source records attributed to S Nakada.

At least 91 records · Page 5Linked to original sources
PubMed1987

IgG and IgE antibodies to Chironomidae in asthmatic patients.

IgG antibodies to Chironomidae and its correlations to radioallergosorbent and skin reactions were examined with the aim of clarifying the relationship between asthma and Chironomidae. The level of specific IgG antibody in asthmatic patients (0.698 +/- 0.034, n = 104) was significantly greater than that in normal subjects (0.367 +/- 0.032, n = 52) (P less than 0.01). The specific IgG level was not correlated to skin reaction, nor to IgE RAST scores. Specific IgG1 and IgG4 levels in asthmatic patients were significantly greater than in control subjects (n = 14) (P less than 0.01).

Animals↗
PubMed1986

Evolution of human influenza A viruses over 50 years: rapid, uniform rate of change in NS gene.

Variation in influenza A viruses was examined by comparison of nucleotide sequences of the NS gene (890 bases) of 15 human viruses isolated over 53 years (1933 to 1985). Changes in the genes accumulate with time, and an evolutionary tree based on the maximum parsimony method can be constructed. The evolutionary rate is approximately 2 X 10(-3) substitution per site per year in the NS genes, which is about 10(6) times the evolutionary rate of germline genes in mammals. This uniform and rapid rate of evolution in the NS gene is a good molecular clock and is compatible with the hypothesis that positive selection is operating on the hemagglutinin (or perhaps some other viral genes) to preserve random mutations in the NS gene.

Base Sequence↗
PubMed1986

Epidemiology of influenza C virus in man: multiple evolutionary lineages and low rate of change.

The nucleotide sequences of nonstructural protein (NS) genes of human influenza C viruses isolated between 1947 and 1983 were determined and compared. Assuming constant evolutionary rates, the extent of nucleotide differences among NS genes does not correspond to the isolation years of the strains. This suggests that more than one gene lineage is present in the population. Furthermore, examination of the eight C virus NS gene sequences by the maximum parsimony method (W. M. Fitch, 1971, Syst. Zool. 20, 406-416) yielded phylogenetic trees that were grossly different from those obtained using the hemagglutinin genes for the same eight isolates. This result is compatible with the idea of reassortment of genes in nature across lineages of influenza C viruses. The sequence analysis also suggests that nucleotide substitutions occur at a lower rate in the C virus NS genes than in influenza A virus NS genes.

Amino Acid Sequence↗
PubMed1986

The influenza C virus NS gene: evidence for a spliced mRNA and a second NS gene product (NS2 protein).

It has previously been shown that the shortest RNA (RNA 7) of influenza C viruses codes for a nonstructural (NSI) protein (Nakada et al. (1985) J. Virol. 56, 221-226). Experiments reported here indicate that RNA 7 also directs the synthesis of a second nonstructural protein via a spliced mRNA. The amino terminal 62 codons of this NS2 protein appear to be shared with the NS1 protein and the carboxyl terminal 59 amino acids are unique (derived from a +1 open reading frame in the mRNA). Although the size of the C virus NS2 protein is comparable to that of the A and B virus NS2 proteins, the overall arrangement of the C virus NS gene is quite different from that of the A and B virus NS genes. The second (+1) open reading frame of the C virus NS gene is completely overlapped by that of the NS1 protein, whereas the second (+1) open reading frame of the A and B virus NS genes extends to the 3' end of the RNA and only partially (or in some strains not at all) overlaps the NS1 open reading frame.

Amino Acid Sequence↗
PubMed1986

Allergenic and immunogenic components of house dust mite, Dermatophagoides farinae.

The house dust mite, Dermatophagoides farinae, was fractionated by a Sephadex G-200 column. Its allergenic (IgE-reacting) and immunogenic (IgG-reacting) components were investigated. By means of skin test, the molecular weight (MW) of major allergenic components of mite was found to be approximately 9,000 to 21,000 daltons. Immunogenic components were investigated by enzyme linked immunosorbent assay using each fraction as an antigen and mice plasma and human serum as antibodies. With mouse plasma, high IgG antibody titers were observed in fractions that contained the part of the mite with high MW (greater than 150,000). With human sera, high IgG antibody titers were observed in fractions that contained the part of the mite with MW more than 30,000. Heterogeneity of human IgG antibody responses against mite antigen was also suggested.

Allergens↗
PubMed1985

Noncumulative sequence changes in the hemagglutinin genes of influenza C virus isolates.

Sequence analysis and comparison of hemagglutinin (HA) genes of different influenza C viruses isolated between 1947 and 1983 reveals that (1) the extent of difference among the HA genes is independent of the year in which these viruses were isolated and that (2) changes in the HA genes do not appear to accumulate with time. These results suggest that epidemiologically dominant variants of influenza C viruses do not emerge successively with time and that C virus variants derived from multiple evolutionary pathways cocirculate at any one time. Thus the epidemiology of influenza C viruses differs markedly from that of influenza A viruses, which is characterized by the emergence of successive variants. Based on the nucleotide sequence data, we propose different evolutionary models for influenza A and influenza C viruses.

Amino Acid Sequence↗
PubMed1985

Effect of mercurials on lymphocyte functions in vitro.

The effect of in vitro treatment with mercurials on several functions of mouse lymphocytes was studied. When lymphocytes were cultured in the presence of mercurials, DNA synthesis induced by mitogen (concanavalin A, phytohemagglutinin-P, lipopolysaccharide) and polyclonal B cell activation induced by lipopolysaccharide were strongly inhibited by methylmercuric chloride at the concentration of 10(-6) M, but mercuric chloride inhibited these functions by 50% at 10(-5) M. Furthermore, 10(-7) M methylmercuric chloride and 10(-6) M mercuric chloride inhibited mixed lymphocyte reaction by 80%. Thus, the inhibitory effect of methylmercuric chloride was 10 times stronger than that of mercuric chloride when the mercurials were present in the culture throughout the incubation. On the other hand, DNA synthesis once induced by mitogens was not significantly affected when 10(-6) M methylmercury was added during the last 3 h of the incubation. Pretreatment with 10(-6) M methylmercury for 1 h, however, showed 50% inhibition of thymidine incorporation into DNA and also reduced the rate of metabolism of phosphatidyl inositol by 50%. These results indicate that methylmercury may act on mouse lymphocytes at an early stage of transformation induced by the mitogens, while inorganic mercury failed to cause the pronounced difference in its potency of inhibition on the functions of lymphocytes by the different treatments of the cells under the various conditions used.

Animals↗
PubMed1985

Expression of influenza virus NS2 nonstructural protein in bacteria and localization of NS2 in infected eucaryotic cells.

The nonstructural NS2 protein of influenza A/PR/8/34 virus was efficiently expressed in bacteria, and monospecific antisera were prepared against the bacterially synthesized polypeptide. These antisera were cross-reactive among the NS2 proteins of various influenza A viruses. However, they did not react with the NS2 of influenza B/Lee/40 virus nor with other proteins of influenza A viruses such as NS1. Antisera against NS2 were used to determine that the NS2 protein is localized in the cell nucleus during influenza virus infection, as shown by immunofluorescence microscopy. Cells infected with simian virus 40 recombinants containing the influenza virus NS gene revealed that both the NS1 and NS2 proteins appeared in the nucleus, even in the absence of expression of other influenza virus-specific components.

Animals↗
PubMed1985

Influenza C virus RNA 7 codes for a nonstructural protein.

The complete nucleotide sequence of RNA segment 7 of influenza C/California/78 virus was determined by using cloned cDNA derived from viral RNA. The gene is 934 nucleotides long and possesses a long open reading frame which can code for a protein of 286 amino acids. Hybrid arrest translation experiments with the cloned cDNA fragment and poly(A)-containing RNA isolated from virus-infected cells showed that a 28,500-molecular-weight protein is coded for by RNA 7. Comparison of the proteins induced in the cell-free system and in virus-infected cells with those found in purified virus suggests that the 28,500-molecular-weight protein is a nonstructural protein.

Amino Acid Sequence↗
PubMed1985

Allergenicity and immunogenicity of house-dust mite (Dermatophagoides farinae) antigens treated with glutaraldehyde.

Extract from house dust mite (Dermatophagoides farinae) was treated with glutaraldehyde (GA) and examined for its allergenicity and immunogenicity. The allergenicity of glutaraldehyde-treated mite extract (GA-M) was decreased significantly when compared with untreated mite extract (UN-M) by skin test in mite allergic individuals. Immunogenicity of GA-M was at least similar with that of UN-M, when examined by formation of antibodies to UN-M in guinea pigs. Fractionations of GA-M and UN-M revealed that polymerization occurred and proteins of higher molecular weight increased after the treatment of mite extract with GA. The results suggest potential usefulness of the polymerized mite antigens in immunotherapy.

Aldehydes↗
PubMed1984

Comparison of automated and conventional keratometers.

Clinical trials in 275 eyes indicated that an automated keratometer (Canon) was equal to or better than a conventional keratometer (Bausch & Lomb). Comparisons of the values obtained with the two instruments showed agreement on the radius of curvature. The automated keratometer detected small differences in directional axis in slightly astigmatic eyes. Because this instrument is quick and simple to operate, it should be widely used, particularly for examining children.

Adolescent↗
PubMed1984

Complete nucleotide sequence of the influenza C/California/78 virus nucleoprotein gene.

The complete nucleotide sequence of RNA segment 5 of the influenza C/California/78 (C/Cal/78) virus was determined by using cloned cDNA derived from viral RNA. The gene contains 1809 nucleotides and can code for a protein of 565 amino acids with a molecular weight of 63 525. The RNA 5 protein of the influenza C/Cal/78 virus possesses two short regions which share a high degree (60-83%) of sequence homology with the nucleoproteins of influenza A and B viruses. These and other structural features of the RNA 5 protein suggest that RNA 5 of influenza C viruses codes for the nucleoprotein. The data also suggest that influenza C viruses are orthomyxoviruses, but that they are more distantly related to either type A or type B viruses than are influenza A and B viruses to each other.

Amino Acid Sequence↗
PubMed1984

Influenza C virus hemagglutinin: comparison with influenza A and B virus hemagglutinins.

The complete nucleotide sequence of the influenza C/California/78 virus RNA 4 was obtained by using cloned cDNA derived from the RNA segment. This gene is 2,071 nucleotides long and can code for a polypeptide of 654 amino acids. Although there are no convincing sequence homologies between RNA 4 and the hemagglutinin genes of influenza A and B viruses, we suggest, on the basis of structural features, that RNA 4 of the influenza C virus codes for the hemagglutinin. The structural features which are common to the hemagglutinins of influenza A, B, and C viruses include (i) a hydrophobic signal peptide, (ii) an arginine cleavage site between the hemagglutinin 1 and 2 subunits, (iii) hydrophobic regions at the amino and carboxyl termini of the hemagglutinin 2 subunit, and (iv) several conserved cysteine residues. Additional evidence that RNA 4 of influenza C virus codes for the hemagglutinin is that the tripeptide Ile-Phe-Gly, known to be present at the amino terminus of the hemagglutinin 2 subunit of influenza C virus, is encoded by RNA 4 at a point immediately adjacent to the presumptive arginine cleavage site. The lack of primary sequence homology between the influenza C virus hemagglutinin and the influenza A or B virus hemagglutinins, which all have similar functions, might be attributed to convergent rather than divergent evolution. However, the structural similarities among the influenza A, B, and C virus hemagglutinins strongly suggest that the three hemagglutinin genes have diverged from a common precursor.

Amino Acid Sequence↗