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T Shioda

Publications and source records attributed to T Shioda.

At least 109 records · Page 6Linked to original sources
PubMed1986

Determination of the complete nucleotide sequence of the Sendai virus genome RNA and the predicted amino acid sequences of the F, HN and L proteins.

We previously determined the 3' proximal 5,824 nucleotides of the Sendai virus genome RNA (Nucleic Acids Res. 11, 7317-7330, 1983; Nucleic Acids Res. 12, 7965-7973, 1984), and present here the sequence of the remaining 5' proximal 9,559 nucleotides. Thus, this is the first paramyxovirus to have its genome organization elucidated. The set of complementary DNA clones used was prepared by the method of Okayama and Berg from polyadenylylated viral genome RNA. We sequenced the region containing the 5' proximal half of the F gene, and the subsequent HN and L genes, and predicted the complete amino acid sequence of the products of these genes. Sequence analyses confirmed that all the genes are flanked by consensus sequences and suggest that the viral mRNAs are capable of forming stem-and-loop structures. Comparison of the F and HN glycoproteins of Sendai virus with those of simian virus 5 strongly suggests that the cysteine residues are highly important for maintenance of the molecular structures of these glycoproteins.

Amino Acid Sequence↗
PubMed1986

Differences in bovine parainfluenza 3 virus variants studied by monoclonal antibodies against viral glycoproteins.

We previously showed that of three bovine parainfluenza 3 virus strains the M strain, which is neurovirulent for young mice, has an extensive syncytium-inducing activity, whereas avirulent SC and 910N strains are weak in this activity. It was also demonstrated that both M and SC strains have very low hemagglutination and neuraminidase activities, while the 910N strain shows these activities to high levels. In the present study, monoclonal antibodies (Mabs) were raised against the glycoproteins of the 910N strain, and utilized to further characterize these three viral strains. Five Mabs against the hemagglutinin-neuraminidase protein, which were classified into four different epitope-recognizing groups, neutralized the M strain much more effectively than the 910N and SC strains, while the Mabs showed lower hemagglutination inhibition (HI) titers against the M and SC strains than the 910N strain. Three Mabs against the fusion protein neutralized the M strain but not the 910N and SC strains, while they showed no HI activity against any of these strains. These findings suggested that the M strain is considerably different from other strains in the structure of the viral envelope proteins.

Animals↗
PubMed1984

Nucleotide sequence of a Sendai virus genome region covering the entire M gene and the 3' proximal 1013 nucleotides of the F gene.

We determined the sequence of the 2,138 nucleotides in the Sendai virus genome just following the 3' proximal 3,686 nucleotides which we had previously reported (Nucleic Acids Res. 11, 7317-7330, 1983). This covers the entire third gene of 1,173 nucleotides and the 3' proximal 1,013 nucleotides of the fourth gene. Like the NP and P+C genes, both the third and fourth genes start from consensus sequence R1 (3'-UCCCAC(or UA)UUUC) at the 3' end and the third gene terminates with consensus sequence R2 (3'-AUUCUUUUU) at the 5' end. The third gene was identified as M, and the deduced 348 amino acids indicated that the M protein is rich in basic residues and has hydrophobic domains near the C-terminal. The fourth gene, although sequencing is not complete yet, was identified as F, since a large open reading frame found in the gene contains the characteristic sequence of 20 amino acids located at the N-terminal of the F1 protein. Analyses of the amino acid sequence suggested that the structure of the F gene product is NH2-signal peptide-F2-F1-COOH.

Animals↗
PubMed1983

Sequence of 3,687 nucleotides from the 3' end of Sendai virus genome RNA and the predicted amino acid sequences of viral NP, P and C proteins.

The sequence of 3,687 nucleotides from the 3' end of the Sendai virus genome (Z strain) was determined by a molecular cloning technique followed by rapid sequence analysis. Two large open reading frames, one consisting of 1,572 nucleotides and the other of 1,704 nucleotides, were observed in the region, that is OP-1 and OP-2 from the 3' end of the genome. The amino acid sequences of the gene products were predicted from the observed sequence. Determination of amino acid compositions of viral proteins, P, HN, Fo, NP and M, led us to conclude that NP and P are the gene products of OP-1 and OP-2, respectively. An additional open reading frame consisting of 612 nucleotides (OP-3) was discovered in the 3' most proximal region of OP-2. The predicted product of OP-3 was considered to be viral non-structural protein C. The leader sequence of 51 nucleotides at the 3' terminal of the genome and consensus sequences at 3' and 5' ends of each gene for proteins NP and P were identified.

Amino Acid Sequence↗
PubMed1983

Neuraminidase activity and syncytial formation in variants of parainfluenza 3 virus.

By a sensitive fluorometric assay method, we could definitely demonstrate neuraminidase activity for two variants of parainfluenza 3 virus, M and SC, which were previously shown to have no detectable neuraminidase activity. The enzyme activities of these viruses were very similar to each other, showing a much lower catalytic rate, a much higher Km value, and a more acidic pH optimum than those of the virus variants of high neuraminidase activity, 910N, LT, and MR. M and SC viruses eluted from guinea pig erythrocytes very poorly, whereas 910N and LT viruses eluted readily. M virus required the aid of a bacterial neuraminidase for effective growth and plaque formation in MDBK cells, but the virus grew well and formed plaques in R66 and Vero cells without the enzyme. SC virus required no exogenous neuraminidase for growth in all of these cell types. Depending on cell type, SC virus induced slight to extensive syncytial formation which was greatly inhibited by exogenous neuraminidase. In contrast, M virus induced extensive syncytial formation in all these cells regardless of the presence or absence of exogenous neuraminidase, although development and disintegration of the syncytia were more or less retarded by the enzyme, especially in MDBK cells. These results indicate that M virus possesses highly potent inducibility of syncytial formation which is further fortified by being low in viral neuraminidase activity.

Adsorption↗
PubMed1981

Cytochemical localization of adenylate cyclase activity in the rat anterior pituitary.

The cytochemical localization of adenylate cyclase was studied in relation to the secretory function of the anterior pituitary glands of male rats. The reaction product of adenylate cyclase was localized on the outside of plasma membranes, but was not detected intracellularly. High activity of adenylate cyclase was detected on somatotrophs and microvilli of follicular cells, whereas no activity was found on thyrotrophs or corticotrophs. Although most of the gonadotrophs showed little or no adenylate-cyclase activity, some was detected in a small number of gonadotrophs in the central portion of the gland. In somatotrophs, activity was not detected on the plasma membranes facing perivascular spaces where exocytotic extrusion of secretory granules was frequently observed, although the remaining areas of plasma membranes of the same somatotrophs were associated with high levels of adenylatle-cyclase activity. These findings indicate that the association of a high level of adenylate-cyclase activity is not directly related to the ability of the plasma membranes to fuse with secretory granule membranes.

Adenylyl Cyclases↗
PubMed1981

Localization of sialic acid-containing hormones in GTH cells and ACTH cells of the rat anterior pituitary.

The localization of sialic acid-containing substances in the rat anterior pituitary gland has been studied by light and electron microscopy, using a peroxidase-labeled lectin (limulus polyphemus agglutinin: LPA) which binds specifically to sialic acid residues. LPA stains two types of anterior pituitary cells: (1) round or ovoid cells which are also positively stained with anti-hCG (GTH cell), and (2) small, stellate cells which are unstained with anti-hCG (ACTH cell). All of the LPA-positive cells can be distinguished from TSH cells which are identified by the use of anti-hTSHbeta. On ultrathin sections directly stained with LPA using the postembedding method, the reaction is confined to the secretory granules in GTH cells, and ACTH cells. Of two types of secretory granules in GTH cells, the larger one is intensely stained, whereas the smaller type shows only weak staining with LPA. Since follicle-stimulating hormone (FSH) is known to have high sialic acid contents, the results suggest possible detection of FSH with a technique other than immunohistochemistry. Furthermore, if the sialic acid-containing substances in GTH cells represents FSH, then these results support the hypothesis that LH cells and FSH cells are one cell type.

Adrenocorticotropic Hormone↗