Chemical and immunological characterization of a low molecular weight outer membrane protein of Salmonella typhi.
Microbiol Immunol
; 42(8): 521-6, 1998.
Article
em En
| MEDLINE
| ID: mdl-9776392
A new immunogenic outer membrane protein, Omp-28 (MW 28,000 and pI 4.6), was isolated from smooth Salmonella typhi cells by the use of an extracting medium containing 6 M urea, 1% deoxycholate and 5 mM EDTA. The purification of Omp-28 was performed by gel filtration and fast ion exchange chromatography. This protein showed to be the prevalent component isolated by the latter methodology. Omp-28 is formed by three identical subunits (MW 9,000), not linked by disulfide bonds. The partial N-terminal amino acid sequence of Omp-28 presented great homology with part of the sequence of an Escherichia coli protein found in a precursor whose sequence was predicted by c-DNA. ELISA and Western blotting identified Omp-28 as the major antigenic protein present in the outer membrane protein fraction, isolated by gel filtration. Antibodies against Omp-28 were detected by ELISA in 43% of 28 sera from typhoid fever convalescent patients. The antisera from mice immunized with Omp-28 and the highest positive typhoid fever convalescent serum gave a positive bactericidal test, killing 50% of Salmonella typhi cells in serum dilutions of 1/80 and 1/320, respectively. These results indicate the immunogenic importance of Omp-28 isolated from Salmonella typhi outer membrane and strongly suggest it should be used in further studies of animal protection against the disease caused by this pathogenic bacteria.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Salmonella typhi
/
Proteínas da Membrana Bacteriana Externa
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Microbiol Immunol
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Austrália