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Production of leptospiral LipL32 antigen in Pichia pastoris and its use in an enzyme-linked immunosorbent assay BABT
Monte,Leonardo Garcia; Leal,Fernanda Munhoz Dos Anjos; Hartwig,Daiane Drawanz; Vasconcellos,Sílvio Arruda; Brihuega,Bibiana; Dellagostin,Odir Antonio; Hartleben,Cláudia Pinho.
The production of recombinant LipL32 protein using Escherichia coli has been used extensively for the development of vaccines and diagnostic tests for leptospirosis. However, E. coli has demonstrated limitations, including low yield and lack of post-translational modifications. In this study, rLipL32 was produced in eukaryotic expression system (Pichia pastoris) and evaluated the antigen by enzyme-linked immunosorbent assay (ELISA). The yield obtained from the culture supernatant reached 270 mg/L and ELISA showed an accuracy of 95.34%. In summary, the production of rLipL32 using P. pastoris did not impair the antigenic characteristics of this antigen and ensured its use for detecting the leptospiral antibodies in swine sera.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Pichia pastoris; LipL32; ELISA; Leptospirosis.
Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000300007
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Expression and purification of the non-tagged LipL32 of pathogenic Leptospira BJMBR
Hauk,P.; Carvalho,E.; Ho,P.L..
Leptospirosis is a reemerging infectious disease and the most disseminated zoonosis worldwide. A leptospiral surface protein, LipL32, only occurs in pathogenic Leptospira, and is the most abundant protein on the bacterial surface, being described as an important factor in host immunogenic response and also in bacterial infection. We describe here an alternative and simple purification protocol for non-tagged recombinant LipL32. The recombinant LipL32(21-272) was expressed in Escherichia coli without His-tag or any other tag used to facilitate recombinant protein purification. The recombinant protein was expressed in the soluble form, and the purification was based on ion exchange (anionic and cationic) and hydrophobic interactions. The final purification...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Antigen; LipL32; Pathogenic Leptospira; Non-tagged protein purification; Diagnosis; Vaccine.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2011000400005
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Diagnosis of canine leptospirosis using an immunomagnetic separation-PCR method BJM
Monte,Leonardo Garcia; Jorge,Sérgio; Luiz,João Paulo Mesquita; Sinnott,Francine; Seixas,Fabiana Kömmling; Aleixo,José Antonio Guimarães; Samartino,Luis Ernesto; Conceição,Fabricio Rochedo; Hartleben,Cláudia Pinho.
Diagnosis of leptospirosis by PCR is hampered due to the presence of substances on biological fluids. Here, we report an immunomagnetic separation step prior to PCR which improved the detection of Leptospira spp. in blood and urine samples from dogs. It resulted in a significant improvement on sensitivity for diagnosis of canine leptospirosis.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Canine leptospirosis; IMS-PCR; LipL32.
Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000200023
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Monoclonal antibodies against an outer membrane protein from pathogenic Leptospira BJM
Lüdtke,Charli Beatriz; Coutinho,Mariana Loner; Jouglard,Sandra Denise Dorneles; Moreira,Cecília Nunes; Fernandes,Cláudia Hartleben Pinho; Brod,Claudiomar Soares; Haake,David A.; Ko,Albert Icksang; Dellagostin,Odir Antonio; Aleixo,José Antonio Guimarães.
Two hybridomas secreting monoclonal antibodies (MAbs) that react with a lipoprotein (LipL32) of the outer membrane of pathogenic Leptospira were obtained. For hybridoma production, spleen cells from BALB/c mice imunized with recombinant LipL32 (rLipL32) were fused to SP2/O-Ag14 cells, selected in HAT medium and screened in an indirect ELISA. One MAb produced was of the IgG2b isotype and the other was an IgM. MAbs specificity was confirmed by indirect ELISA and immunoblotting using purified rLipL32 and whole-cell antigen preparations from Escherichia coli (E. coli) expressing LipL32 and from pathogenic and non-pathogenic serovars. Both Mabs reacted with most of the pathogenic serovars tested and none reacted with non-pathogenic Leptospira. The MAbs...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Leptospirosis; Monoclonal antibodies; LipL32.
Ano: 2003 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822003000500001
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Characterization of Leptospira borgpetersenii isolates from field rats (Rattus norvegicus) by 16S rRNA and lipL32 gene sequencing BJM
Vedhagiri,Kumaresan; Natarajaseenivasan,Kalimuthusamy; Prabhakaran,Shanmugarajan G.; Selvin,Joseph; Narayanan,Ramasamy; Shouche,Yogesh S.; Vijayachari,Paluru; Ratnam,Sivalingam.
The main goal of this study was to evaluate the prevalence of leptospirosis among field rodents of Tiruchirappalli district, Tamil Nadu, India. In total 35 field rats were trapped and tested for seroprevalence by the microscopic agglutination test (MAT). Isolation of leptospires was performed from blood and kidney tissues and characterized to serovar level. Genomospecies identification was carried out using 16S rRNA and lipL32 gene sequencing. The molecular phylogeny was constructed to find out species segregation. Seroprevalence was about 51.4 %, and the predominant serovars were Autumnalis, Javanica, Icterohaemorrhagiae and Pomona. Two isolates from the kidneys were identified as serovar Javanica of Serogroup Javanica, and sequence based molecular...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Leptospirosis; Leptospira borgpetersenii; LipL32; 16S rRNA.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822010000100022
Registros recuperados: 5
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