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Score: 6.00 |
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| Title: In vivo and in vitro phosphorylation of rice dwarf phytoreovirus Pns12 cytoplasmic nonstructural protein .
| | Journal: Arch . Virol . Citation: V : 144 ( 7 ) P : 1371-80 Year: | | Literature: oryza Field: abstract Doc ID: pub10481743 Accession (PMID): 10481743 | | Abstract: In vivo and in vitro phosphorylation and intracellular location of rice dwarf phytoreovirus Pns12 , which is encoded by one of the twelve dsRNA genome segments , S12 , and comprises 312 amino acids , was investigated .
When [ 32P ] phosphoric acid was incorporated into RDV-infected leafhopper cultured cells , labelled Pns12 was immunoprecipitated from the cells by a monospecific anti-Pns12 polyclonal antibody .
Recombinant Pns12 was purified from Spodoptera frugiperda cells infected with AcRS12 , a baculovirus recombinant carrying a full-length cDNA of RDV S12 .
Purified Pns12 was also demonstrated to be phosphorylated in vitro by a kinase activity present in host ( rice , barley , wheat , leafhopper ) cells and non-host ( tobacco , spinach , white clover , S frugiperda , mosquito , mammals ) cells as well .
Immunocytochemical studies showed Pns12 accumulated in the cytoplasm of infected cells , and frequently localized in a slightly electron-dense patch .
These results demonstrated that RDV Pns12 was a cytoplasmic nonstructural phosphoprotein . | Matching Sentences:
[ Sen. 1, subscore: 1.00 ]: In vivo and in vitro phosphorylation and intracellular location of rice dwarf phytoreovirus Pns12 , which is encoded by one of the twelve dsRNA genome segments , S12 , and comprises 312 amino acids , was investigated . When [ 32P ] phosphoric acid was incorporated into RDV-infected leafhopper cultured cells , labelled Pns12 was immunoprecipitated from the cells by a monospecific anti-Pns12 polyclonal antibody . Recombinant Pns12 was purified from Spodoptera frugiperda cells infected with AcRS12 , a baculovirus recombinant carrying a full-length cDNA of RDV S12 . Purified Pns12 was also demonstrated to be phosphorylated in vitro by a kinase activity present in host ( rice , barley , wheat , leafhopper ) cells and non-host ( tobacco , spinach , white clover , S frugiperda , mosquito , mammals ) cells as well . Immunocytochemical studies showed Pns12 accumulated in the cytoplasm of infected cells , and frequently localized in a slightly electron-dense patch .
[ Sen. 2, subscore: 1.00 ]: In vivo and in vitro phosphorylation and intracellular location of rice dwarf phytoreovirus Pns12 , which is encoded by one of the twelve dsRNA genome segments , S12 , and comprises 312 amino acids , was investigated . When [ 32P ] phosphoric acid was incorporated into RDV-infected leafhopper cultured cells , labelled Pns12 was immunoprecipitated from the cells by a monospecific anti-Pns12 polyclonal antibody . Recombinant Pns12 was purified from Spodoptera frugiperda cells infected with AcRS12 , a baculovirus recombinant carrying a full-length cDNA of RDV S12 . Purified Pns12 was also demonstrated to be phosphorylated in vitro by a kinase activity present in host ( rice , barley , wheat , leafhopper ) cells and non-host ( tobacco , spinach , white clover , S frugiperda , mosquito , mammals ) cells as well . Immunocytochemical studies showed Pns12 accumulated in the cytoplasm of infected cells , and frequently localized in a slightly electron-dense patch . These results demonstrated that RDV Pns12 was a cytoplasmic nonstructural phosphoprotein .
[ Sen. 3, subscore: 1.00 ]: In vivo and in vitro phosphorylation and intracellular location of rice dwarf phytoreovirus Pns12 , which is encoded by one of the twelve dsRNA genome segments , S12 , and comprises 312 amino acids , was investigated . When [ 32P ] phosphoric acid was incorporated into RDV-infected leafhopper cultured cells , labelled Pns12 was immunoprecipitated from the cells by a monospecific anti-Pns12 polyclonal antibody . Recombinant Pns12 was purified from Spodoptera frugiperda cells infected with AcRS12 , a baculovirus recombinant carrying a full-length cDNA of RDV S12 . Purified Pns12 was also demonstrated to be phosphorylated in vitro by a kinase activity present in host ( rice , barley , wheat , leafhopper ) cells and non-host ( tobacco , spinach , white clover , S frugiperda , mosquito , mammals ) cells as well . Immunocytochemical studies showed Pns12 accumulated in the cytoplasm of infected cells , and frequently localized in a slightly electron-dense patch . These results demonstrated that RDV Pns12 was a cytoplasmic nonstructural phosphoprotein .
[ Sen. 4, subscore: 1.00 ]: In vivo and in vitro phosphorylation and intracellular location of rice dwarf phytoreovirus Pns12 , which is encoded by one of the twelve dsRNA genome segments , S12 , and comprises 312 amino acids , was investigated . When [ 32P ] phosphoric acid was incorporated into RDV-infected leafhopper cultured cells , labelled Pns12 was immunoprecipitated from the cells by a monospecific anti-Pns12 polyclonal antibody . Recombinant Pns12 was purified from Spodoptera frugiperda cells infected with AcRS12 , a baculovirus recombinant carrying a full-length cDNA of RDV S12 . Purified Pns12 was also demonstrated to be phosphorylated in vitro by a kinase activity present in host ( rice , barley , wheat , leafhopper ) cells and non-host ( tobacco , spinach , white clover , S frugiperda , mosquito , mammals ) cells as well . Immunocytochemical studies showed Pns12 accumulated in the cytoplasm of infected cells , and frequently localized in a slightly electron-dense patch . These results demonstrated that RDV Pns12 was a cytoplasmic nonstructural phosphoprotein .
[ Sen. 5, subscore: 1.00 ]: In vivo and in vitro phosphorylation and intracellular location of rice dwarf phytoreovirus Pns12 , which is encoded by one of the twelve dsRNA genome segments , S12 , and comprises 312 amino acids , was investigated . When [ 32P ] phosphoric acid was incorporated into RDV-infected leafhopper cultured cells , labelled Pns12 was immunoprecipitated from the cells by a monospecific anti-Pns12 polyclonal antibody . Recombinant Pns12 was purified from Spodoptera frugiperda cells infected with AcRS12 , a baculovirus recombinant carrying a full-length cDNA of RDV S12 . Purified Pns12 was also demonstrated to be phosphorylated in vitro by a kinase activity present in host ( rice , barley , wheat , leafhopper ) cells and non-host ( tobacco , spinach , white clover , S frugiperda , mosquito , mammals ) cells as well . Immunocytochemical studies showed Pns12 accumulated in the cytoplasm of infected cells , and frequently localized in a slightly electron-dense patch . These results demonstrated that RDV Pns12 was a cytoplasmic nonstructural phosphoprotein .
[ Sen. 6, subscore: 1.00 ]: When [ 32P ] phosphoric acid was incorporated into RDV-infected leafhopper cultured cells , labelled Pns12 was immunoprecipitated from the cells by a monospecific anti-Pns12 polyclonal antibody . Recombinant Pns12 was purified from Spodoptera frugiperda cells infected with AcRS12 , a baculovirus recombinant carrying a full-length cDNA of RDV S12 . Purified Pns12 was also demonstrated to be phosphorylated in vitro by a kinase activity present in host ( rice , barley , wheat , leafhopper ) cells and non-host ( tobacco , spinach , white clover , S frugiperda , mosquito , mammals ) cells as well . Immunocytochemical studies showed Pns12 accumulated in the cytoplasm of infected cells , and frequently localized in a slightly electron-dense patch . These results demonstrated that RDV Pns12 was a cytoplasmic nonstructural phosphoprotein .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 3.00 |
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| Title: Glutelin basic subunits have a mammalian mucin-type O-linked disaccharide side chain .
| | Journal: Arch . Biochem . Biophys . Citation: V : 370 ( 2 ) P : 271-7 Year: 1999 | | Literature: oryza Field: abstract Doc ID: pub10510286 Accession (PMID): 10510286 | | Abstract: Characterization was done on the sugar chains of glutelin , a major storage protein in rice seeds .
The basic subunits of glutelin were shown to be glycoproteins by staining with PAS and the lectins concanavalin A ( Con A ) and peanut agglutinin ( PNA ) .
The binding of PNA to the basic subunits was substantially reduced by treatment of the glutelin with NaIO4 , NaOH , or O-glycanase .
The sugar chains of the subunits , obtained by hydrazinolysis and O-glycanase , were pyridylaminated and subjected to 2-dimensional HPLC analysis using C ( 18 ) and acrylamide-derivatized columns .
It was found that the Galbeta-1 , 3GalNAc disaccharide , which was previously identified as a core 1 structure of mucin-type sugar chains , is conjugated to the glutelin subunits .
Furthermore , amino acid sequencing of an 11-kDa peptide of the subunits , recognized by both PNA and Con A , suggested that both N-linked and O-linked glycosylation occurs in the carboxy-terminal region of these subunits . | Matching Sentences:
[ Sen. 2, subscore: 1.00 ]: Characterization was done on the sugar chains of glutelin , a major storage protein in rice seeds . The basic subunits of glutelin were shown to be glycoproteins by staining with PAS and the lectins concanavalin A ( Con A ) and peanut agglutinin ( PNA ) . The binding of PNA to the basic subunits was substantially reduced by treatment of the glutelin with NaIO4 , NaOH , or O-glycanase . The sugar chains of the subunits , obtained by hydrazinolysis and O-glycanase , were pyridylaminated and subjected to 2-dimensional HPLC analysis using C ( 18 ) and acrylamide-derivatized columns . It was found that the Galbeta-1 , 3GalNAc disaccharide , which was previously identified as a core 1 structure of mucin-type sugar chains , is conjugated to the glutelin subunits . Furthermore , amino acid sequencing of an 11-kDa peptide of the subunits , recognized by both PNA and Con A , suggested that both N-linked and O-linked glycosylation occurs in the carboxy-terminal region of these subunits .
[ Sen. 3, subscore: 1.00 ]: Characterization was done on the sugar chains of glutelin , a major storage protein in rice seeds . The basic subunits of glutelin were shown to be glycoproteins by staining with PAS and the lectins concanavalin A ( Con A ) and peanut agglutinin ( PNA ) . The binding of PNA to the basic subunits was substantially reduced by treatment of the glutelin with NaIO4 , NaOH , or O-glycanase . The sugar chains of the subunits , obtained by hydrazinolysis and O-glycanase , were pyridylaminated and subjected to 2-dimensional HPLC analysis using C ( 18 ) and acrylamide-derivatized columns . It was found that the Galbeta-1 , 3GalNAc disaccharide , which was previously identified as a core 1 structure of mucin-type sugar chains , is conjugated to the glutelin subunits . Furthermore , amino acid sequencing of an 11-kDa peptide of the subunits , recognized by both PNA and Con A , suggested that both N-linked and O-linked glycosylation occurs in the carboxy-terminal region of these subunits .
[ Sen. 6, subscore: 1.00 ]: The basic subunits of glutelin were shown to be glycoproteins by staining with PAS and the lectins concanavalin A ( Con A ) and peanut agglutinin ( PNA ) . The binding of PNA to the basic subunits was substantially reduced by treatment of the glutelin with NaIO4 , NaOH , or O-glycanase . The sugar chains of the subunits , obtained by hydrazinolysis and O-glycanase , were pyridylaminated and subjected to 2-dimensional HPLC analysis using C ( 18 ) and acrylamide-derivatized columns . It was found that the Galbeta-1 , 3GalNAc disaccharide , which was previously identified as a core 1 structure of mucin-type sugar chains , is conjugated to the glutelin subunits . Furthermore , amino acid sequencing of an 11-kDa peptide of the subunits , recognized by both PNA and Con A , suggested that both N-linked and O-linked glycosylation occurs in the carboxy-terminal region of these subunits .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 6.00 |
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| Title: Developmentally regulated expression of a peptide : N-glycanase during germination of rice seeds ( Oryza sativa ) and its purification and characterization .
| | Journal: J Biol . Chem . Citation: V : 275 ( 1 ) P : 129-34 Year: 2000 | | Literature: oryza Field: abstract Doc ID: pub10617595 Accession (PMID): 10617595 | | Abstract: Peptide : N-glycanase ( PNGase ; EC 3 . 5 . 1 . 52 ) activity was detected in dormant rice seeds ( Oryza sativa ) and the imbibed rice grains .
Time-course studies revealed that the enzyme activity remained almost constant until about 30 h after imbibition in both of endosperm and embryo it issue-containing areas , and started to increase only in growing germ part , reached a peak at about 3-day stage , followed by a gradual decrease concomitant with a sharp increase in the coleoptile .
The specific activity increased about 6-fold at about 3-day stage .
PNGase was purified to electrophoretic homogeneity from the extracts of germinated rice seeds at 24 h , and the apparent molecular weight of the purified enzyme , estimated by SDS-polyacrylamide gel electrophoresis ( SDS-PAGE ) , was about 80 , 000 .
The purified enzyme was designated PNGase Os to denote its origin .
The N-terminal sequence of the 10 residues was determined to be SYNVASVAGL .
The purified PNGase Os in SDS-PAGE appeared as a rather broad band , consistent with the presence of multiple glycoforms as indicated by chromatographic behavior on a Sephadex G-75 column .
PNGase expressed in coleoptile under anoxia condition was also purified , and both of the purified enzymes were found to exhibit very similar , if not identical , electrophoretic mobility in SDS-PAGE .
PNGase Os exhibited a broad pH-activity profile with an optimum of 4-5 and , interestingly , was significantly inactivated by K ( + ) and Na ( + ) at near the physiological concentration , 100 mM .
These results are discussed in relation to other work . | Matching Sentences:
[ Sen. 1, subscore: 1.00 ]: Peptide : N-glycanase ( PNGase ; EC 3 . 5 . 1 . 52 ) activity was detected in dormant rice seeds ( Oryza sativa ) and the imbibed rice grains . Time-course studies revealed that the enzyme activity remained almost constant until about 30 h after imbibition in both of endosperm and embryo it issue-containing areas , and started to increase only in growing germ part , reached a peak at about 3-day stage , followed by a gradual decrease concomitant with a sharp increase in the coleoptile . The specific activity increased about 6-fold at about 3-day stage . PNGase was purified to electrophoretic homogeneity from the extracts of germinated rice seeds at 24 h , and the apparent molecular weight of the purified enzyme , estimated by SDS-polyacrylamide gel electrophoresis ( SDS-PAGE ) , was about 80 , 000 . The purified enzyme was designated PNGase Os to denote its origin .
[ Sen. 4, subscore: 1.00 ]: Peptide : N-glycanase ( PNGase ; EC 3 . 5 . 1 . 52 ) activity was detected in dormant rice seeds ( Oryza sativa ) and the imbibed rice grains . Time-course studies revealed that the enzyme activity remained almost constant until about 30 h after imbibition in both of endosperm and embryo it issue-containing areas , and started to increase only in growing germ part , reached a peak at about 3-day stage , followed by a gradual decrease concomitant with a sharp increase in the coleoptile . The specific activity increased about 6-fold at about 3-day stage . PNGase was purified to electrophoretic homogeneity from the extracts of germinated rice seeds at 24 h , and the apparent molecular weight of the purified enzyme , estimated by SDS-polyacrylamide gel electrophoresis ( SDS-PAGE ) , was about 80 , 000 . The purified enzyme was designated PNGase Os to denote its origin . The N-terminal sequence of the 10 residues was determined to be SYNVASVAGL . The purified PNGase Os in SDS-PAGE appeared as a rather broad band , consistent with the presence of multiple glycoforms as indicated by chromatographic behavior on a Sephadex G-75 column . PNGase expressed in coleoptile under anoxia condition was also purified , and both of the purified enzymes were found to exhibit very similar , if not identical , electrophoretic mobility in SDS-PAGE .
[ Sen. 5, subscore: 1.00 ]: Peptide : N-glycanase ( PNGase ; EC 3 . 5 . 1 . 52 ) activity was detected in dormant rice seeds ( Oryza sativa ) and the imbibed rice grains . Time-course studies revealed that the enzyme activity remained almost constant until about 30 h after imbibition in both of endosperm and embryo it issue-containing areas , and started to increase only in growing germ part , reached a peak at about 3-day stage , followed by a gradual decrease concomitant with a sharp increase in the coleoptile . The specific activity increased about 6-fold at about 3-day stage . PNGase was purified to electrophoretic homogeneity from the extracts of germinated rice seeds at 24 h , and the apparent molecular weight of the purified enzyme , estimated by SDS-polyacrylamide gel electrophoresis ( SDS-PAGE ) , was about 80 , 000 . The purified enzyme was designated PNGase Os to denote its origin . The N-terminal sequence of the 10 residues was determined to be SYNVASVAGL . The purified PNGase Os in SDS-PAGE appeared as a rather broad band , consistent with the presence of multiple glycoforms as indicated by chromatographic behavior on a Sephadex G-75 column . PNGase expressed in coleoptile under anoxia condition was also purified , and both of the purified enzymes were found to exhibit very similar , if not identical , electrophoretic mobility in SDS-PAGE . PNGase Os exhibited a broad pH-activity profile with an optimum of 4-5 and , interestingly , was significantly inactivated by K ( + ) and Na ( + ) at near the physiological concentration , 100 mM .
[ Sen. 7, subscore: 1.00 ]: The specific activity increased about 6-fold at about 3-day stage . PNGase was purified to electrophoretic homogeneity from the extracts of germinated rice seeds at 24 h , and the apparent molecular weight of the purified enzyme , estimated by SDS-polyacrylamide gel electrophoresis ( SDS-PAGE ) , was about 80 , 000 . The purified enzyme was designated PNGase Os to denote its origin . The N-terminal sequence of the 10 residues was determined to be SYNVASVAGL . The purified PNGase Os in SDS-PAGE appeared as a rather broad band , consistent with the presence of multiple glycoforms as indicated by chromatographic behavior on a Sephadex G-75 column . PNGase expressed in coleoptile under anoxia condition was also purified , and both of the purified enzymes were found to exhibit very similar , if not identical , electrophoretic mobility in SDS-PAGE . PNGase Os exhibited a broad pH-activity profile with an optimum of 4-5 and , interestingly , was significantly inactivated by K ( + ) and Na ( + ) at near the physiological concentration , 100 mM . These results are discussed in relation to other work .
[ Sen. 8, subscore: 1.00 ]: PNGase was purified to electrophoretic homogeneity from the extracts of germinated rice seeds at 24 h , and the apparent molecular weight of the purified enzyme , estimated by SDS-polyacrylamide gel electrophoresis ( SDS-PAGE ) , was about 80 , 000 . The purified enzyme was designated PNGase Os to denote its origin . The N-terminal sequence of the 10 residues was determined to be SYNVASVAGL . The purified PNGase Os in SDS-PAGE appeared as a rather broad band , consistent with the presence of multiple glycoforms as indicated by chromatographic behavior on a Sephadex G-75 column . PNGase expressed in coleoptile under anoxia condition was also purified , and both of the purified enzymes were found to exhibit very similar , if not identical , electrophoretic mobility in SDS-PAGE . PNGase Os exhibited a broad pH-activity profile with an optimum of 4-5 and , interestingly , was significantly inactivated by K ( + ) and Na ( + ) at near the physiological concentration , 100 mM . These results are discussed in relation to other work .
[ Sen. 9, subscore: 1.00 ]: The purified enzyme was designated PNGase Os to denote its origin . The N-terminal sequence of the 10 residues was determined to be SYNVASVAGL . The purified PNGase Os in SDS-PAGE appeared as a rather broad band , consistent with the presence of multiple glycoforms as indicated by chromatographic behavior on a Sephadex G-75 column . PNGase expressed in coleoptile under anoxia condition was also purified , and both of the purified enzymes were found to exhibit very similar , if not identical , electrophoretic mobility in SDS-PAGE . PNGase Os exhibited a broad pH-activity profile with an optimum of 4-5 and , interestingly , was significantly inactivated by K ( + ) and Na ( + ) at near the physiological concentration , 100 mM . These results are discussed in relation to other work .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 2.00 |
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| Title: Genotypic characterization of drug-resistant Mycobacterium tuberculosis isolates from Peru .
| | Journal: Tuber .
Lung Dis .
Citation: V : 79 ( 2 ) P : 111-8 Year: | | Literature: oryza Field: abstract Doc ID: pub10645449 Accession (PMID): 10645449 | | Abstract: SETTING : Twenty-nine epidemiological unrelated and mostly multidrug-resistant Mycobacterium tuberculosis ( MDR-TB ) strains from Peruvian patients .
OBJECTIVE : To investigate the molecular genetics of MDR-TB strains recovered in a Latin American country .
DESIGN : Antimicrobial agent susceptibility testing , major genetic group designation , IS6110 fingerprinting , spoligotyping , and automated deoxyribonucleic acid sequencing of regions of the katG , rpoB , embB , gyrA , and pncA genes with mutations commonly associated with drug resistance .
RESULTS : Nineteen isolates were found to be multidrug-resistant by susceptibility testing .
IS6110 typing showed that virtually all isolates were unique and therefore had independently acquired drug resistance .
Seventy-nine percent of isoniazid-resistant strains had a Ser315Thr amino acid change in KatG .
Ninety-five percent of rifampin-resistant isolates had amino acid replacements in the rifampin-resistance determining region of RpoB .
Six of 11 ethambutol-resistant strains had EmbB alterations .
Eleven pyrazinamide-resistant strains had distinct mutations in pncA .
CONCLUSION : Virtually all organisms evolved drug resistance independently .
The types of drug resistance-associated mutations identified were very similar to changes occurring in isolates from other areas of the world .
Nucleotide sequence-based strategies for rapid detection of drug resistance-conferring mutants will be applicable to organisms recovered in Peru , and potentially other areas of Latin America . | Matching Sentences:
[ Sen. 3, subscore: 1.00 ]: SETTING : Twenty-nine epidemiological unrelated and mostly multidrug-resistant Mycobacterium tuberculosis ( MDR-TB ) strains from Peruvian patients . OBJECTIVE : To investigate the molecular genetics of MDR-TB strains recovered in a Latin American country . DESIGN : Antimicrobial agent susceptibility testing , major genetic group designation , IS6110 fingerprinting , spoligotyping , and automated deoxyribonucleic acid sequencing of regions of the katG , rpoB , embB , gyrA , and pncA genes with mutations commonly associated with drug resistance . RESULTS : Nineteen isolates were found to be multidrug-resistant by susceptibility testing . IS6110 typing showed that virtually all isolates were unique and therefore had independently acquired drug resistance . Seventy-nine percent of isoniazid-resistant strains had a Ser315Thr amino acid change in KatG . Ninety-five percent of rifampin-resistant isolates had amino acid replacements in the rifampin-resistance determining region of RpoB .
[ Sen. 9, subscore: 1.00 ]: IS6110 typing showed that virtually all isolates were unique and therefore had independently acquired drug resistance . Seventy-nine percent of isoniazid-resistant strains had a Ser315Thr amino acid change in KatG . Ninety-five percent of rifampin-resistant isolates had amino acid replacements in the rifampin-resistance determining region of RpoB . Six of 11 ethambutol-resistant strains had EmbB alterations . Eleven pyrazinamide-resistant strains had distinct mutations in pncA . CONCLUSION : Virtually all organisms evolved drug resistance independently . The types of drug resistance-associated mutations identified were very similar to changes occurring in isolates from other areas of the world . Nucleotide sequence-based strategies for rapid detection of drug resistance-conferring mutants will be applicable to organisms recovered in Peru , and potentially other areas of Latin America .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 2.00 |
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| Title: Sequence analysis of Pns11 , a nonstructural protein of rice gall dwarf virus , and its expression and detection in infected rice plants and vector insects .
| | Journal: Virus Genes Citation: V : 20 ( 3 ) P : 237-41 Year: | | Literature: oryza Field: abstract Doc ID: pub10949951 Accession (PMID): 10949951 | | Abstract: The nucleotide sequence of genome segment S11 of rice gall dwarf virus ( RGDV ) , a member of Phytoreovirus , was determined .
The segment encodes a putative protein of 40 kDa that exhibits approximately 37% homology at the amino acid level to the nonstructural proteins Pns10 of rice dwarf and wound tumor viruses , which are other members of Phytoreovirus .
A band of a protein with an apparent molecular mass of 40 kDa was specifically detected in an analysis of cells transfected with S11 cDNA .
An antiserum raised against this protein reacted with a protein of approximately 40kDa after fractionation by SDS-PAGE of materials prepared from infected plants and from viruliferous vector insects .
However , the antiserum did not react with purified viral proteins .
These results suggest that S11 encodes a nonstructural protein of RGDV .
This protein was named Pns11 . | Matching Sentences:
[ Sen. 2, subscore: 1.00 ]: The nucleotide sequence of genome segment S11 of rice gall dwarf virus ( RGDV ) , a member of Phytoreovirus , was determined . The segment encodes a putative protein of 40 kDa that exhibits approximately 37% homology at the amino acid level to the nonstructural proteins Pns10 of rice dwarf and wound tumor viruses , which are other members of Phytoreovirus . A band of a protein with an apparent molecular mass of 40 kDa was specifically detected in an analysis of cells transfected with S11 cDNA . An antiserum raised against this protein reacted with a protein of approximately 40kDa after fractionation by SDS-PAGE of materials prepared from infected plants and from viruliferous vector insects . However , the antiserum did not react with purified viral proteins . These results suggest that S11 encodes a nonstructural protein of RGDV .
[ Sen. 7, subscore: 1.00 ]: A band of a protein with an apparent molecular mass of 40 kDa was specifically detected in an analysis of cells transfected with S11 cDNA . An antiserum raised against this protein reacted with a protein of approximately 40kDa after fractionation by SDS-PAGE of materials prepared from infected plants and from viruliferous vector insects . However , the antiserum did not react with purified viral proteins . These results suggest that S11 encodes a nonstructural protein of RGDV . This protein was named Pns11 .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 3.00 |
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| Title: Sequencing of the rpoB gene in Legionella pneumophila and characterization of mutations associated with rifampin resistance in the Legionellaceae .
| | Journal: Antimicrob .
Agents Chemother .
Citation: V : 44 ( 10 ) P : 2679-83 Year: 2000 | | Literature: oryza Field: abstract Doc ID: pub10991843 Accession (PMID): 10991843 | | Abstract: Rifampin in combination with erythromycin is a recommended treatment for severe cases of legionellosis .
Mutations in the rpoB gene are known to cause rifampin resistance in Escherichia coli and Mycobacterium tuberculosis , and the purpose of the present study was to investigate a possible similar resistance mechanism within the members of the family Legionellaceae .
Since the RNA polymerase genes of this genus have never been characterized , the DNA sequence of the Legionella pneumophila rpoB gene was determined by the Vectorette technique for genome walking .
A 4 , 647-bp DNA sequence that contained the open reading frame ( ORF ) of the rpoB gene ( 4 , 104 bp ) and an ORF of 384 bp representing part of the rpoC gene was obtained .
A 316-bp DNA fragment in the center of the L pneumophila rpoB gene , corresponding to a previously described site for mutations leading to rifampin resistance in M tuberculosis , was sequenced from 18 rifampin-resistant Legionella isolates representing four species ( L bozemanii , L longbeachae , L micdadei , and L pneumophila ) , and the sequences were compared to the sequences of the fragments from the parent ( rifampin-sensitive ) strains .
Six single-base mutations which led to amino acid substitutions at five different positions were identified .
A single strain did not contain any mutations in the 316-bp fragment .
This study represents the characterization of a hitherto undescribed resistance mechanism within the family Legionellaceae . | Matching Sentences:
[ Sen. 5, subscore: 2.00 ]: Rifampin in combination with erythromycin is a recommended treatment for severe cases of legionellosis . Mutations in the rpoB gene are known to cause rifampin resistance in Escherichia coli and Mycobacterium tuberculosis , and the purpose of the present study was to investigate a possible similar resistance mechanism within the members of the family Legionellaceae . Since the RNA polymerase genes of this genus have never been characterized , the DNA sequence of the Legionella pneumophila rpoB gene was determined by the Vectorette technique for genome walking . A 4 , 647-bp DNA sequence that contained the open reading frame ( ORF ) of the rpoB gene ( 4 , 104 bp ) and an ORF of 384 bp representing part of the rpoC gene was obtained . A 316-bp DNA fragment in the center of the L pneumophila rpoB gene , corresponding to a previously described site for mutations leading to rifampin resistance in M tuberculosis , was sequenced from 18 rifampin-resistant Legionella isolates representing four species ( L bozemanii , L longbeachae , L micdadei , and L pneumophila ) , and the sequences were compared to the sequences of the fragments from the parent ( rifampin-sensitive ) strains . Six single-base mutations which led to amino acid substitutions at five different positions were identified . A single strain did not contain any mutations in the 316-bp fragment . This study represents the characterization of a hitherto undescribed resistance mechanism within the family Legionellaceae .
[ Sen. 3, subscore: 1.00 ]: Rifampin in combination with erythromycin is a recommended treatment for severe cases of legionellosis . Mutations in the rpoB gene are known to cause rifampin resistance in Escherichia coli and Mycobacterium tuberculosis , and the purpose of the present study was to investigate a possible similar resistance mechanism within the members of the family Legionellaceae . Since the RNA polymerase genes of this genus have never been characterized , the DNA sequence of the Legionella pneumophila rpoB gene was determined by the Vectorette technique for genome walking . A 4 , 647-bp DNA sequence that contained the open reading frame ( ORF ) of the rpoB gene ( 4 , 104 bp ) and an ORF of 384 bp representing part of the rpoC gene was obtained . A 316-bp DNA fragment in the center of the L pneumophila rpoB gene , corresponding to a previously described site for mutations leading to rifampin resistance in M tuberculosis , was sequenced from 18 rifampin-resistant Legionella isolates representing four species ( L bozemanii , L longbeachae , L micdadei , and L pneumophila ) , and the sequences were compared to the sequences of the fragments from the parent ( rifampin-sensitive ) strains . Six single-base mutations which led to amino acid substitutions at five different positions were identified . A single strain did not contain any mutations in the 316-bp fragment .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 1.00 |
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| Title: Genotypic determination of Mycobacterium tuberculosis antibiotic resistance using a novel mutation detection method , the branch migration inhibition M tuberculosis antibiotic resistance test | | Journal: J Clin . Microbiol . Citation: V : 38 ( 10 ) P : 3656-62 Year: 2000 | | Literature: oryza Field: abstract Doc ID: pub11015379 Accession (PMID): 11015379 | | Abstract: A novel method for the detection of any alteration within a defined sequence has recently been demonstrated ( A Lishanski , N Kurn , and E F Ullman , Nucleic Acids Res .
28 : E42 , 2000 ; A Lishanski , Clin . Chem . 46 : 9 , 2000 ) .
Essential to this method are the generation of partial duplexes that are capable of forming four-stranded structures and the ability to detect inhibition of branch migration in these structures ( I G Panyutin and P Hsieh , J Mol . Biol . 230 : 413-424 , 1993 ) .
Inhibition of branch migration indicates the presence of sequence alteration .
This mutation detection method , termed branch migration inhibition ( BMI ) , is suitable for the detection of drug resistance in M tuberculosis , which is frequently associated with multiple mutations within known genes .
We describe the genotypic determination of the rifampin ( RMP ) and pyrazinamide ( PZA ) susceptibilities of M tuberculosis isolates , using BMI coupled with the luminescence oxygen channeling immunoassay ( LOCI ) ( E F Ullman et al , Proc . Natl . Acad . Sci . USA 91 : 5426-5430 , 1994 ) .
RMP and PZA resistances are associated with multiple mutations within the rpoB and pncA genes , respectively .
M tuberculosis genomic DNA samples prepared from 46 clinical isolates were used for genotypic determination of RMP resistance in a "blind study . " Similarly , PZA resistance was determined using genomic DNA samples prepared from 37 clinical isolates .
Full agreement of the genotypic and phenotypic determinations of drug susceptibility was demonstrated .
RMP susceptibility determination directly from cells of 10 clinical isolates grown in culture was also demonstrated .
The genotypic result of only 1 out of 10 isolates did not agree with the phenotypic susceptibility testing result .
Sequence analysis of the rpoB gene of this clinical isolate revealed a single base substitution , most likely a silent point mutation .
The new BMI-LOCI mutation detection method is a rapid and accurate procedure for the genotypic determination of the RMP and PZA susceptibilities of M tuberculosis clinical isolates .
BMI can also be detected by using commercially available automated enzyme-linked immunosorbent assay plate formats ( Lishanski et al , Nucleic Acids Res .
28 : E42 , 2000 ) . | Matching Sentences:
[ Sen. 7, subscore: 1.00 ]: Essential to this method are the generation of partial duplexes that are capable of forming four-stranded structures and the ability to detect inhibition of branch migration in these structures ( I G Panyutin and P Hsieh , J Mol . Biol . 230 : 413-424 , 1993 ) . Inhibition of branch migration indicates the presence of sequence alteration . This mutation detection method , termed branch migration inhibition ( BMI ) , is suitable for the detection of drug resistance in M tuberculosis , which is frequently associated with multiple mutations within known genes . We describe the genotypic determination of the rifampin ( RMP ) and pyrazinamide ( PZA ) susceptibilities of M tuberculosis isolates , using BMI coupled with the luminescence oxygen channeling immunoassay ( LOCI ) ( E F Ullman et al , Proc . Natl . Acad . Sci . USA 91 : 5426-5430 , 1994 ) . RMP and PZA resistances are associated with multiple mutations within the rpoB and pncA genes , respectively . M tuberculosis genomic DNA samples prepared from 46 clinical isolates were used for genotypic determination of RMP resistance in a "blind study . " Similarly , PZA resistance was determined using genomic DNA samples prepared from 37 clinical isolates . Full agreement of the genotypic and phenotypic determinations of drug susceptibility was demonstrated . RMP susceptibility determination directly from cells of 10 clinical isolates grown in culture was also demonstrated . The genotypic result of only 1 out of 10 isolates did not agree with the phenotypic susceptibility testing result .
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Score: 2.00 |
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| Title: [ A patient with dysphagia treated successfully and discharged without nutritional support ] | | Journal: Gan To Kagaku Ryoho Citation: V : 27 Suppl 3 ( ) P : 754-5 Year: 2000 | | Literature: oryza Field: abstract Doc ID: pub11190340 Accession (PMID): 11190340 | | Abstract: One of the main targets of medical care provided in our ward , which specializes in the cooperative practice of hospital and home-doctors , is to maintain the quality of patients lives after they are discharged from our hospital through home medical care by home-doctors .
Intravenous hyperalimentation and tube-feeding at home are suitable solutions for some patients with dysphagia after cerebral infarction .
However , the difficulties faced in their management are the burden on the families , which tends to be an obstacle for at-home-practice .
We describe herein a case of severe dysphagia treated successfully through our rehabilitation program and discharged without nutritional supports .
An 82-year-old man was admitted to our hospital suffering from pyrexia and dysbasia .
The man , who lives with his wife and his sons family , was diagnosed with aspiration pneumonia and multiple cerebral infarctions .
The test for swallowing reflex revealed an impaired first phase reflex and intravenous hyperalimentation was performed for his nutritional support .
He was still suffering from dysphagia but had the desire to eat orally after his dysbasia and aspiration pneumonia were cured .
A rehabilitation program was scheduled with the aims of 1 ) recovery of ingestion and 2 ) sufficient expectoration , with an ongoing teaching program for the management of intravenous hyperalimentation .
After one month of rehabilitation ( ice-massaging , muscle rehabilitation of the tongue and neck and expectoration training in a prone position and after gorging ) , his ability to swallow was gradually recovered .
With the frequent confirmation of absence of aspiration , special forms of diets were served and upgraded from jelly , paste-like-food to soft-cooked steamed rice .
The patient is now at home without any nutritional support .
Nutritional management without intravenous hyperalimentation or tube-feeding is important or even essential for some families providing home-care for patients .
The problem of aging requires us to reduce the burden that families ( who may be also getting older ) should carry .
We try to support patients and families for better home-care through cooperation with society and home-doctors .
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[ Sen. 6, subscore: 1.00 ]: Intravenous hyperalimentation and tube-feeding at home are suitable solutions for some patients with dysphagia after cerebral infarction . However , the difficulties faced in their management are the burden on the families , which tends to be an obstacle for at-home-practice . We describe herein a case of severe dysphagia treated successfully through our rehabilitation program and discharged without nutritional supports . An 82-year-old man was admitted to our hospital suffering from pyrexia and dysbasia . The man , who lives with his wife and his sons family , was diagnosed with aspiration pneumonia and multiple cerebral infarctions . The test for swallowing reflex revealed an impaired first phase reflex and intravenous hyperalimentation was performed for his nutritional support . He was still suffering from dysphagia but had the desire to eat orally after his dysbasia and aspiration pneumonia were cured . A rehabilitation program was scheduled with the aims of 1 ) recovery of ingestion and 2 ) sufficient expectoration , with an ongoing teaching program for the management of intravenous hyperalimentation . After one month of rehabilitation ( ice-massaging , muscle rehabilitation of the tongue and neck and expectoration training in a prone position and after gorging ) , his ability to swallow was gradually recovered .
[ Sen. 8, subscore: 1.00 ]: We describe herein a case of severe dysphagia treated successfully through our rehabilitation program and discharged without nutritional supports . An 82-year-old man was admitted to our hospital suffering from pyrexia and dysbasia . The man , who lives with his wife and his sons family , was diagnosed with aspiration pneumonia and multiple cerebral infarctions . The test for swallowing reflex revealed an impaired first phase reflex and intravenous hyperalimentation was performed for his nutritional support . He was still suffering from dysphagia but had the desire to eat orally after his dysbasia and aspiration pneumonia were cured . A rehabilitation program was scheduled with the aims of 1 ) recovery of ingestion and 2 ) sufficient expectoration , with an ongoing teaching program for the management of intravenous hyperalimentation . After one month of rehabilitation ( ice-massaging , muscle rehabilitation of the tongue and neck and expectoration training in a prone position and after gorging ) , his ability to swallow was gradually recovered . With the frequent confirmation of absence of aspiration , special forms of diets were served and upgraded from jelly , paste-like-food to soft-cooked steamed rice . The patient is now at home without any nutritional support .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 2.00 |
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| Title: Transposon impala , a novel tool for gene tagging in the rice blast fungus Magnaporthe grisea .
| | Journal: Mol .
Plant Microbe Interact .
Citation: V : 14 ( 3 ) P : 308-15 Year: 2001 | | Literature: oryza Field: abstract Doc ID: pub11277428 Accession (PMID): 11277428 | | Abstract: impala , a Tc1-mariner transposable element from Fusarium oxysporum , was introduced into the rice blast fungus Magnaporthe grisea to develop transposon-based insertional mutagenesis .
A construct ( pNIL160 ) containing an autonomous impala copy inserted in the promoter of niaD encoding Aspergillus nidulans nitrate reductase was introduced by transformation into a M grisea nitrate reductase-deficient mutant . impala excision was monitored by restoration of prototrophy for nitrate .
Southern analysis of niaD+ revertants revealed that impala was able to excise and reinsert at new loci in M grisea .
As observed for its host Fusarium oxysporum , impala inserted at a TA site left a typical excision footprint of 5 bp .
We have shown that a defective impala copy was inactive in M grisea , yet it can be activated by a functional impala transposase .
A transformant carrying a single copy of pNIL160 was used to generate a collection of 350 revertants .
Mutants either altered for their mycelial growth ( Rev2 ) or nonpathogenic ( Rev77 ) were obtained .
Complementation of Rev77 with a 3-kb genomic fragment from a wild-type locus was successful , demonstrating the tagging of a pathogenicity gene by impala .
This gene , called ORP1 , is essential for penetration of host leaves by M grisea and has no sequence homology to known genes . | Matching Sentences:
[ Sen. 2, subscore: 1.00 ]: impala , a Tc1-mariner transposable element from Fusarium oxysporum , was introduced into the rice blast fungus Magnaporthe grisea to develop transposon-based insertional mutagenesis . A construct ( pNIL160 ) containing an autonomous impala copy inserted in the promoter of niaD encoding Aspergillus nidulans nitrate reductase was introduced by transformation into a M grisea nitrate reductase-deficient mutant . impala excision was monitored by restoration of prototrophy for nitrate . Southern analysis of niaD+ revertants revealed that impala was able to excise and reinsert at new loci in M grisea . As observed for its host Fusarium oxysporum , impala inserted at a TA site left a typical excision footprint of 5 bp . We have shown that a defective impala copy was inactive in M grisea , yet it can be activated by a functional impala transposase . A transformant carrying a single copy of pNIL160 was used to generate a collection of 350 revertants .
[ Sen. 6, subscore: 1.00 ]: A construct ( pNIL160 ) containing an autonomous impala copy inserted in the promoter of niaD encoding Aspergillus nidulans nitrate reductase was introduced by transformation into a M grisea nitrate reductase-deficient mutant . impala excision was monitored by restoration of prototrophy for nitrate . Southern analysis of niaD+ revertants revealed that impala was able to excise and reinsert at new loci in M grisea . As observed for its host Fusarium oxysporum , impala inserted at a TA site left a typical excision footprint of 5 bp . We have shown that a defective impala copy was inactive in M grisea , yet it can be activated by a functional impala transposase . A transformant carrying a single copy of pNIL160 was used to generate a collection of 350 revertants . Mutants either altered for their mycelial growth ( Rev2 ) or nonpathogenic ( Rev77 ) were obtained . Complementation of Rev77 with a 3-kb genomic fragment from a wild-type locus was successful , demonstrating the tagging of a pathogenicity gene by impala . This gene , called ORP1 , is essential for penetration of host leaves by M grisea and has no sequence homology to known genes .
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Score: 1.00 |
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| Title: Rice alpha-mannosidase digesting the high mannose glycopeptide of glutelin .
| | Journal: Citation: V : 112 ( 1 ) P : 15-24 Year: 2001 | | Literature: oryza Field: abstract Doc ID: pub11319010 Accession (PMID): 11319010 | | Abstract: alpha-Mannosidase ( EC 3 . 2 . 1 . 24 ) from rice dry seeds was purified to homogeneity .
Optimum pH and Km for pNP-alpha-Man hydrolysis were pH 4 . 3-4 . 5 and 1 . 04 mM , respectively .
The enzyme digested mannobioses such as Manalpha-1 , 2Man , Manalpha-1 , 6Man , Manalpha-1 , 3Man but Manalpha-1 , 4Man .
Zn2+ ion was required for the activity , whereas EDTA and swainsonine inhibited the activity by 80 and 96% , respectively .
The rice storage protein , glutelin was prepared and its basic subunits were shown to have high mannose-type sugar chains by two-dimensional mapping using NH2-P and C18 silica columns .
They were Man9GlcNAc2 , Man8GlcNAc2 , Man7GlcNAc2 , Man6GlcNAc2 and Man5GlcNAc2 .
All these oligosaccharides were digested by the purified alpha-mannosidase , and Man-GlcNAc2 and mannose were formed .
Glycopeptides , having these high mannose-type sugar chains , could also be digested by the alpha-mannosidase .
Subunits were prepared from glutelin basic subunit and the richest subunit among them , subunit 2 ( isoform 2 ) , was digested by the alpha-mannosidase .
Isoform 2 was digested by V8 protease only partially and slowly .
However , isoform 2 , pre-treated with the alpha-mannosidase , was rapidly and completely digested by V8 protease .
| Matching Sentences:
[ Sen. 2, subscore: 1.00 ]: alpha-Mannosidase ( EC 3 . 2 . 1 . 24 ) from rice dry seeds was purified to homogeneity . Optimum pH and Km for pNP-alpha-Man hydrolysis were pH 4 . 3-4 . 5 and 1 . 04 mM , respectively . The enzyme digested mannobioses such as Manalpha-1 , 2Man , Manalpha-1 , 6Man , Manalpha-1 , 3Man but Manalpha-1 , 4Man . Zn2+ ion was required for the activity , whereas EDTA and swainsonine inhibited the activity by 80 and 96% , respectively . The rice storage protein , glutelin was prepared and its basic subunits were shown to have high mannose-type sugar chains by two-dimensional mapping using NH2-P and C18 silica columns . They were Man9GlcNAc2 , Man8GlcNAc2 , Man7GlcNAc2 , Man6GlcNAc2 and Man5GlcNAc2 .
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