Characterization of the gene encoding the MPB51, one of the major secreted protein antigens of Mycobacterium bovis BCG, and identification of the secreted protein closely related to the fibronectin binding 85 complex

Naoya Oohara, H. Kitaura, H. Hotokezaka, T. Nishiyama, N. Wada, S. Matsumoto, T. Matsuo, M. Naito, T. Yamada

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

The secreted protein MPB51 is one of the major proteins in the culture filtrate of Mycobacterium bovis BCG (BCG) and is a protein immunologically cross-reacting with the fibronectin binding 85 complex secreted by this bacterium. The gene encoding MPB51 (mpb51) was cloned, sequenced, and expressed in Escherichia coli. The mpb51 gene was mapped downstream of the gene for 85A component with 179 bp spaces. The mpb51 gene encoded 299 amino acids, including 33 amino acids for the signal peptide, followed by 266 amino acids for the mature protein with a molecular mass of 27807.37 Da. This is the first complete sequence of MPB51. MPB51 showed 37-43% homology to the components of 85 complex. Two-dimensional electrophoresis of culture fluids of BCG and Western blotting indicated the existence of the other novel protein(s) which strongly cross-reacted with the α antigen (85B) and MPB51.

Original languageEnglish
Pages (from-to)433-442
Number of pages10
JournalScandinavian Journal of Immunology
Volume41
Issue number5
Publication statusPublished - 1995
Externally publishedYes

Fingerprint

Mycobacterium bovis
Fibronectins
Antigens
Genes
Proteins
Amino Acids
Gene Components
Protein Sorting Signals
Electrophoresis
Western Blotting
Escherichia coli
Bacteria

ASJC Scopus subject areas

  • Immunology

Cite this

Characterization of the gene encoding the MPB51, one of the major secreted protein antigens of Mycobacterium bovis BCG, and identification of the secreted protein closely related to the fibronectin binding 85 complex. / Oohara, Naoya; Kitaura, H.; Hotokezaka, H.; Nishiyama, T.; Wada, N.; Matsumoto, S.; Matsuo, T.; Naito, M.; Yamada, T.

In: Scandinavian Journal of Immunology, Vol. 41, No. 5, 1995, p. 433-442.

Research output: Contribution to journalArticle

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abstract = "The secreted protein MPB51 is one of the major proteins in the culture filtrate of Mycobacterium bovis BCG (BCG) and is a protein immunologically cross-reacting with the fibronectin binding 85 complex secreted by this bacterium. The gene encoding MPB51 (mpb51) was cloned, sequenced, and expressed in Escherichia coli. The mpb51 gene was mapped downstream of the gene for 85A component with 179 bp spaces. The mpb51 gene encoded 299 amino acids, including 33 amino acids for the signal peptide, followed by 266 amino acids for the mature protein with a molecular mass of 27807.37 Da. This is the first complete sequence of MPB51. MPB51 showed 37-43{\%} homology to the components of 85 complex. Two-dimensional electrophoresis of culture fluids of BCG and Western blotting indicated the existence of the other novel protein(s) which strongly cross-reacted with the α antigen (85B) and MPB51.",
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AU - Oohara, Naoya

AU - Kitaura, H.

AU - Hotokezaka, H.

AU - Nishiyama, T.

AU - Wada, N.

AU - Matsumoto, S.

AU - Matsuo, T.

AU - Naito, M.

AU - Yamada, T.

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AB - The secreted protein MPB51 is one of the major proteins in the culture filtrate of Mycobacterium bovis BCG (BCG) and is a protein immunologically cross-reacting with the fibronectin binding 85 complex secreted by this bacterium. The gene encoding MPB51 (mpb51) was cloned, sequenced, and expressed in Escherichia coli. The mpb51 gene was mapped downstream of the gene for 85A component with 179 bp spaces. The mpb51 gene encoded 299 amino acids, including 33 amino acids for the signal peptide, followed by 266 amino acids for the mature protein with a molecular mass of 27807.37 Da. This is the first complete sequence of MPB51. MPB51 showed 37-43% homology to the components of 85 complex. Two-dimensional electrophoresis of culture fluids of BCG and Western blotting indicated the existence of the other novel protein(s) which strongly cross-reacted with the α antigen (85B) and MPB51.

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