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PMID: 7631144 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Homology between the MPB70 and MPB83 proteins of Mycobacterium bovis BCG.

Scandinavian journal of immunology ·Vol. 42 ·No. 1 ·1995-07-00 ·Pages 46-51

Harboe M, Nagai S, Wiker HG, Sletten K, Haga S

Abstract

Isolation of MPB83 from Mycobacterium bovis BCG Tokyo culture fluid is described. MPB70 and MPB83 have similar molecular mass as judged by SDS-PAGE but differ in isoelectric points. Peptides isolated after CNBr cleavage of MPB83 revealed extensive homology as well as distinct differences from corresponding parts of the amino acid sequence deduced from the mpb70 gene cloned by Terasaka et al. Antibodies produced by immunization with MPB70 and MPB83 had distinctly different fine specificity revealing cross-reactivity between the proteins. These findings indicate that two distinct, homologous genes code for these proteins. Sensitization with live BCG Tokyo also induced T cell responses to MPB83 with development of delayed type hypersensitivity in guinea pigs.

MeSH Terms
Amino Acid Sequence Antigens, Bacterial Bacterial Proteins/analysis,chemistry,immunology,isolation & purification Cross Reactions Isoelectric Focusing Membrane Proteins Molecular Sequence Data Mycobacterium bovis/chemistry Sequence Homology, Amino Acid
Chemicals
Antigens, Bacterial Bacterial Proteins MPB83 protein, Mycobacterium Membrane Proteins MPB70 protein, Mycobacterium bovis
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Harboe M
Institute of Immunology and Rheumatology, University of Oslo, Norway.
Nagai S
Wiker H G
Sletten K
Haga S
Article Info
Journal
Scandinavian journal of immunology
Abbr.
Scand J Immunol
ISSN
0300-9475
Published
1995-07-00
Pages
46-51
Language
English
Region
England
NLM ID
0323767
Subset
IM
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