Serological expression cloning and immunological evaluation of MTB48, a novel Mycobacterium tuberculosis antigen

Detalhes bibliográficos
Autor(a) principal: Lodes, Michael J.
Data de Publicação: 2001
Outros Autores: Dillon, Davin C., Mohamath, Raodoh, Day, Craig H., Benson, Darin R., Sampaio, Diana Pedral, Badaró, Roberto José da Silva
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UFBA
Texto Completo: http://www.repositorio.ufba.br/ri/handle/ri/7724
Resumo: Texto completo: acesso restrito. p. 2485-2493
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spelling Lodes, Michael J.Dillon, Davin C.Mohamath, RaodohDay, Craig H.Benson, Darin R.Sampaio, Diana PedralBadaró, Roberto José da SilvaLodes, Michael J.Dillon, Davin C.Mohamath, RaodohDay, Craig H.Benson, Darin R.Sampaio, Diana PedralBadaró, Roberto José da Silva2013-01-03T15:18:32Z20010095-1137http://www.repositorio.ufba.br/ri/handle/ri/7724v. 39, n. 7Texto completo: acesso restrito. p. 2485-2493Improved diagnostics are needed for the detection ofMycobacterium tuberculosis, especially for patients with smear-negative disease. To address this problem, we have screenedM. tuberculosis (H37Rv and Erdman strains) genomic expression libraries with pooled sera from patients with extrapulmonary disease and with sera from patients with elevated reactivity withM. tuberculosis lysate. Both serum pools were reactive with clones expressing a recombinant protein referred to here as MTB48. The genomic sequence of the resulting clones was identical to that of the M. tuberculosis H37Rv isolate and showed 99% identity to the Mycobacterium bovis and M. bovis BCG isolate sequences. The genomic location of this sequence is 826 bp upstream of a region containing theesat-6 gene that is deleted in the M. bovis BCG isolate. The mtb48 1,380-bp open reading frame encodes a predicted 47.6-kDa polypeptide with no known function. Southern and Western blot analyses indicate that this sequence is present in a single copy and is conserved in the M. tuberculosis and M. bovis isolates tested but not in other mycobacterial species tested, includingMycobacterium leprae and Mycobacterium avium. In addition, the native protein was detected in the cytoplasm, as was a processed form that was also shed into the medium during culture. Serological analysis of recombinant MTB48 and theM. tuberculosis 38-kDa antigen with a panel of patient and control sera indicates that the inclusion of recombinant MTB48 in a prototype serodiagnostic test increases assay sensitivity for M. tuberculosis infection when it is combined with other known immunodominant antigens, such as the 38-kDa antigen.Submitted by Suelen Reis (suelen_suzane@hotmail.com) on 2013-01-03T15:18:32Z No. of bitstreams: 1 Lodes.pdf: 850822 bytes, checksum: 632711e9f8603a4cda6c7c4384e099fc (MD5)Made available in DSpace on 2013-01-03T15:18:32Z (GMT). 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dc.title.pt_BR.fl_str_mv Serological expression cloning and immunological evaluation of MTB48, a novel Mycobacterium tuberculosis antigen
dc.title.alternative.pt_BR.fl_str_mv Journal of Clinical Mircobiology
title Serological expression cloning and immunological evaluation of MTB48, a novel Mycobacterium tuberculosis antigen
spellingShingle Serological expression cloning and immunological evaluation of MTB48, a novel Mycobacterium tuberculosis antigen
Lodes, Michael J.
title_short Serological expression cloning and immunological evaluation of MTB48, a novel Mycobacterium tuberculosis antigen
title_full Serological expression cloning and immunological evaluation of MTB48, a novel Mycobacterium tuberculosis antigen
title_fullStr Serological expression cloning and immunological evaluation of MTB48, a novel Mycobacterium tuberculosis antigen
title_full_unstemmed Serological expression cloning and immunological evaluation of MTB48, a novel Mycobacterium tuberculosis antigen
title_sort Serological expression cloning and immunological evaluation of MTB48, a novel Mycobacterium tuberculosis antigen
author Lodes, Michael J.
author_facet Lodes, Michael J.
Dillon, Davin C.
Mohamath, Raodoh
Day, Craig H.
Benson, Darin R.
Sampaio, Diana Pedral
Badaró, Roberto José da Silva
author_role author
author2 Dillon, Davin C.
Mohamath, Raodoh
Day, Craig H.
Benson, Darin R.
Sampaio, Diana Pedral
Badaró, Roberto José da Silva
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Lodes, Michael J.
Dillon, Davin C.
Mohamath, Raodoh
Day, Craig H.
Benson, Darin R.
Sampaio, Diana Pedral
Badaró, Roberto José da Silva
Lodes, Michael J.
Dillon, Davin C.
Mohamath, Raodoh
Day, Craig H.
Benson, Darin R.
Sampaio, Diana Pedral
Badaró, Roberto José da Silva
description Texto completo: acesso restrito. p. 2485-2493
publishDate 2001
dc.date.issued.fl_str_mv 2001
dc.date.accessioned.fl_str_mv 2013-01-03T15:18:32Z
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dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.uri.fl_str_mv http://www.repositorio.ufba.br/ri/handle/ri/7724
dc.identifier.issn.none.fl_str_mv 0095-1137
dc.identifier.number.pt_BR.fl_str_mv v. 39, n. 7
identifier_str_mv 0095-1137
v. 39, n. 7
url http://www.repositorio.ufba.br/ri/handle/ri/7724
dc.language.iso.fl_str_mv eng
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