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1.
Parasite Immunol ; 34(1): 1-7, 2012 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-21929686

RESUMO

The present work describes the isolation and purification of two Leishmania chagasi (= syn. Leishmania infantum) recombinant proteins, rLci2B and rLci1A, and their use in the development of an immunoassay for the diagnostic of canine leishmaniasis. After protein expression and cell disruption, rLci2B was purified by immobilized metal affinity chromatography followed by size exclusion chromatography, whereas rLci1A, expressed as an inclusion body, was treated with urea and purified by anion-exchange chromatography. Homogeneities were ascertained by denaturing gel electrophoresis (MW (rLci2B) = 46,370; MW(rLci1A) = 88,400), isoelectric focusing (pI (rLci2B) = 5·91; pI (rLci1A) = 6·01) and Western blot. An indirect ELISA was developed using the purified antigens rLci2B and rLci1A and a leishmaniasis canine serum panel (n = 256). The ELISA showed 100% sensitivity and 95% specificity for rLci2B and 96% sensitivity and 92% specificity for rLci1A. The purified proteins did not present cross-reactivity with sera from dogs infected with Trypanosoma caninum, Babesia canis and Ehrlichia canis. Cross-reaction was verified with sera from dogs infected with Leishmania brasiliensis (11·7% for rLci2B and 2·9% for rLci1A). Based on ELISA results, it is suggested the use of rLci2B and rLci1A as antigens in an alternative serological assay for diagnostic of canine leishmania.


Assuntos
Anticorpos Antiprotozoários/sangue , Antígenos de Protozoários , Doenças do Cão/diagnóstico , Leishmania infantum/imunologia , Leishmaniose/veterinária , Animais , Antígenos de Protozoários/genética , Antígenos de Protozoários/isolamento & purificação , Cromatografia de Afinidade/métodos , Cromatografia por Troca Iônica/métodos , Reações Cruzadas , Cães , Ensaio de Imunoadsorção Enzimática/métodos , Leishmania infantum/genética , Leishmaniose/diagnóstico , Proteínas Recombinantes , Sensibilidade e Especificidade
2.
Vaccine ; 25(41): 7261-70, 2007 Oct 10.
Artigo em Inglês | MEDLINE | ID: mdl-17719147

RESUMO

The steps to produce, purify and control an immunogenic Brazilian conjugate vaccine against group C meningococcus (MenCPS-TT) using hydrazide-activated tetanus toxoid were developed. The conjugation methodology reduced the reaction time easily allowing scale-up. One freeze-dried pilot vaccine lot purified by tangential filtration, showed satisfactory quality control results including safety and stability. The pilot vaccine was immunogenic in mice in a dose-dependent fashion generating a 10-20-fold rise in IgG response in mice. The vaccine also induced high bactericidal titers. Vaccine concentrations of 1 and 0.1 microg showed higher avidity indices, suggesting induction of immunologic memory. These results support initiation of Phase I clinical studies with the MenCPS-TT conjugate vaccine.


Assuntos
Vacinas Meningocócicas/imunologia , Toxoide Tetânico/imunologia , Animais , Anticorpos Antibacterianos/sangue , Afinidade de Anticorpos , Relação Dose-Resposta Imunológica , Estabilidade de Medicamentos , Filtração/métodos , Imunoglobulina G/sangue , Vacinas Meningocócicas/química , Vacinas Meningocócicas/isolamento & purificação , Vacinas Meningocócicas/toxicidade , Camundongos , Viabilidade Microbiana , Toxoide Tetânico/química , Toxoide Tetânico/metabolismo
3.
Stud Health Technol Inform ; 51: 204-9, 1998.
Artigo em Inglês | MEDLINE | ID: mdl-10179623

RESUMO

This article makes an approach about the use of multimedia resources applied in odontology computer science educational, especially in periodontia. It highlights the importance of the use of these resources, as well as the one that than there is of more recent in this area.


Assuntos
Instrução por Computador , Multimídia , Periodontia/educação , Humanos
4.
FEMS Immunol Med Microbiol ; 15(2-3): 159-68, 1996 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-8880142

RESUMO

Two monoclonal antibodies (mAbs) were produced against a serogroup B Neisseria meningitidis strain. These mAbs recognized two epitopes in the class 5 outer membrane proteins (OMP), designated P5.7 and P5.Bm, and were able to kill the homologous strain through complement activation. Both epitopes were surface exposed and 68% of group B meningococcal clinical isolates had one or both epitopes present in their class 5 OMP. Antibodies to one or both epitopes were demonstrated in 17 patients with meningococcal meningitis using an ELISA inhibition assay. Of the 17 paired sera, 41% and 29% of the acute-phase sera had antibodies to the P5.7 and P5.Bm epitopes, respectively. Immunoglobulin G to P5.Bm were found in all 17 convalescent-phase sera while specific antibodies against P5.7 were only found in 6 of these sera. These results demonstrate the potential importance of the P5.Bm and P5.7 epitopes on the class 5 OMP as candidates for vaccine composition.


Assuntos
Anticorpos Antibacterianos/sangue , Antígenos de Bactérias/imunologia , Proteínas da Membrana Bacteriana Externa/imunologia , Meningite Meningocócica/imunologia , Neisseria meningitidis/imunologia , Anticorpos Monoclonais/imunologia , Especificidade de Anticorpos , Ensaio de Imunoadsorção Enzimática , Epitopos/imunologia , Humanos
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