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Registros recuperados: 46
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Characterization of a leucine aminopeptidase from Toxoplasma gondii OAK
Jia, Honglin; Nishikawa, Yoshifumi; Luo, Yuzi; Yamagishi, Junya; Sugimoto, Chihiro; Xuan, Xuenan.
The M17 family leucine aminopeptidase (LAP) hydrolyze amino acids from the N-terminus of peptides. Many LAPs from parasitic protozoa including Plasmmodium, Trypanosoma and Leishmania, have been intensely investigated because of their crucial roles in parasite biology. In this study, a functional recombinant Toxoplasma gondii LAP (rTgLAP) was expressed in Escherichia coli and its enzymatic activity against synthetic substrates for aminopeptidase, as well as the cellular localization was determined. Our results indicated that TgLAP is a functional aminopeptidase in the cytoplasma of T. gondii.
Palavras-chave: Toxoplasma gondii; Leucine aminopeptidase; Enzymatic activity.
Ano: 2010 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/2822
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Identification and characterization of cross-reactive antigens from Neospora caninum and Toxoplasma gondii OAK
Liao, Min; Xuan, Xuenan; Huang, Xiaohong; Shirafuji, Hiroaki; Fukumoto, Shinya; Hirata, Haruyuki; Suzuki, Hiroshi; Fujisaki, Kozo.
Murine monoclonal antibodies (mAbs) against Neospora caninum tachyzoites were produced to identify the cross-reactive antigens between N. caninum and Toxoplasma gondii. Ten mAbs recognizing cross-reactive antigens of both parasites were obtained and tentatively classified into 6 different groups based on their reactivity patterns in an indirect fluorescent antibody test and Western blot analysis. Three mAbs in group I recognized antigens located on the surface of parasites with molecular masses ranging from 28 to 76 kDa; one mAb in group 2 recognized antigens located on interior organelles of parasites with a molecular mass of 50 kDa; one mAb in group 3 recognized antigens located on interior organelles of parasites with molecular masses of 35 kDa and 14...
Palavras-chave: Neospora caninum; Toxoplasma gondii; Cross-reactive antigen; Protein disulfide isomerase; Heat-shock protein; Ribosomal protein 1.
Ano: 2005 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/816
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Identification of ribosomal phosphoprotein P0 of Neospora caninum as a potential common vaccine candidate for the control of both neosporosis and toxoplasmosis OAK
Zhang, Houshuang; Lee, Eung-goo; Liao, Min; Compaore, Muller K.A.; Zhang, Guohong; Kawase, Osamu; Fujisaki, Kozo; Sugimoto, Chihiro; Nishikawa, Yoshifumi; Xuan, Xuenan.
The characterization of the cross-reactive antigens of two closely related apicomplexan parasites, Neospora caninum and Toxoplasma gondii, is important to elucidate the common mechanisms of parasite–host interactions. In this context, a gene encoding N. caninum ribosomal phosphoprotein P0 (NcP0) was identified by immunoscreening of a N. caninum tachyzoite cDNA expression library with antisera from mice immunized with T. gondii tachyzoites. The NcP0 was encoded by a gene with open reading frame of 936 bp, which encoded a protein of 311 amino acids. The NcP0 gene existed as a single copy in the genome and was interrupted by a 432 bp intron. The NcP0 showed 94.5% amino acid identity to T. gondii P0 (TgP0). Anti-recombinant NcP0 (rNcP0) sera recognized a...
Palavras-chave: Neospora caninum; Toxoplasma gondii; Ribosomal phosphoprotein P0; Cross-reactive.
Ano: 2007 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/1035
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Artesunate, a potential drug for treatment of Babesia infection OAK
Goo, Youn-Kyoung; Terkawi, M. Alaa; Jia, Honglin; Aboge, G. Oluga; Ooka, Hideo; Kim, Suk; Igarashi, Ikuo; Nishikawa, Yoshifumi; Xuan, Xuenan.
The effect of artesunate, a water-soluble artemisinin derivative, against Babesia species, such as Babesia bovis, Babesia gibsoni, and Babesia microti was studied. Cultures of B. bovis and B. gibsoni were treated with 0.26 μM, 2.6 μM, 26 μM, and 260 μM artesunate, and the growth-inhibitory effect was shown in over 2.6 μM artesunate in day 4 and day 3 post-subculture for B. bovis and B. gibsoni, respectively, in dose-dependent manner. In vivo experiment for B. microti, strong inhibition effects were observed in mouse groups treated with over 1.0 mg/kg body weight of artesunate on day 9 and 10 post-infection. These results suggest that artesunate could be a potential drug for Babesia infection.
Palavras-chave: Artesunate; Babesia bovis; Babesia gibsoni; Babesia microti.
Ano: 2010 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/2820
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Detection of Antibodies to Babesia equi by The Latex Agglutination Test with Recombinant Merozoite Antigen-2 OAK
Tanaka, Tetsuya; Xuan, Xuenan; Igarashi, Ikuo; Nagasawa, Hideyuki; Fujisaki, Kozo; Suzuki, Naoyoshi; Mikami, Takeshi; 玄, 学南; 五十嵐, 郁男.
Palavras-chave: Babesia equi; EMA-2; Baculovirus; Latex agglutination test.
Ano: 1999 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/329
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Babesia gibsoni ribosomal phosphoprotein P0 induces cross-protective immunity against B-microti infection in mice OAK
Terkawi, M. Alaa; Jia, Honglin; Zhou, Jinlin; Lee, Eung-goo; Igarashi, Ikuo; Fujisaki, Kozo; Nishikawa, Yoshifumi; Xuan, Xuenan.
Babesia gibsoni ribosomal phosphoprotein PO (BgP0) was identified as an immunodominant cross-reactive antigen with B. microti. The BgPO gene is a single copy with a predicted open reading frame of 942 bp and 314 amino acids. The BgP0 was expressed as a glutathione S-transferase fusion protein in Escherichia coli. The serum raised in mice with the recombinant BgPO showed a specific band with a 34-kDa molecular mass in the extracts of B. gibsoni and B. microti merozoites. Furthermore, the intraperitoneal (i.p.) immunization of rBgP0 and Freund's adjuvant induced strong Immoral response consisting of mixed immunoglobulins IgG1 and IgG2a in BALB/c mice. Following the challenge with B. microti, these mice delayed the onset of parasites and significantly reduced...
Palavras-chave: B. gibsoni; B. microti; Ribosomal phosphoprotein P0; Cross-reactive antigen.
Ano: 2007 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/1036
Registros recuperados: 46
Primeira ... 123 ... Última
 

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