Immunogens of Brucella Abortus S19 Identified By Two-Dimensional Gel Electrophoresis and Immunoblotting
Authors
Abstract:
Background: Lipopolysaccharides (LPSs) and several antigenic proteins of Brucella have been considered for preparation of diagnostic reagents and subunit vaccines. The objective of this study was to identify and compare immunogens of B. abortus S19 which induce humoral immune responses in human, goat and rabbit. Material and Methods: The bacterial whole cell extract was prepared in extraction buffer and resolved using two-dimensional gel electrophoresis (2-DE). The resolved antigens were reacted against human, goat and rabbit sera using western blotting. Results: At least 19, 14 and 16 immunogenic proteins were recognized in western blotting with human, goat and rabbit sera, respectively. The most abundant proteins of the bacterium with immunogenic properties in goat and rabbit but not in human, were a group of 5-6 proteins with molecular masses of 32-34 KDa and isoelectric point (pI) ranging from 4.5 to 5.7. In contrast, a group of 5 proteins with molecular weight of 45 KDa and pI in the range of 4.5 to 5.4 as well as several low molecular weight proteins were immunogenic in human. Furthermore several proteins of Brucella had similar reactions against all sera. Conclusion: These results showed that some of the antigenic proteins of Brucella could be candidates for more accurate diagnosis of Brucellosis in humans and domestic animals.Iran J Med Sci 2005; 30(1): 10-15. Keywords ● Brucella abortus ● Two dimensional gel electrophoresis ● Immunoblot ● Immunogens
similar resources
immunogens of brucella abortus s19 identified by two-dimensional gel electrophoresis and immunoblotting
background: lipopolysaccharides (lpss) and several antigenic proteins of brucella have been considered for preparation of diagnostic reagents and subunit vaccines. the objective of this study was to identify and compare immunogens of b. abortus s19 which induce humoral immune responses in human, goat and rabbit. material and methods: the bacterial whole cell extract was prepared in extraction...
full textAntigens of Brucella abortus S19 immunodominant for bovine lymphocytes as identified by one- and two-dimensional cellular immunoblotting.
Cellular immune responses are influential for protection against intracellular bacteria such as brucellae. Therefore, identification of Brucella abortus antigens that activate primed bovine lymphocytes is fundamental for discerning the breadth of cellular response in bovine brucellosis. Potentially antigenic components of B. abortus S19 were isolated by sodium dodecyl sulfate-polyacrylamide gel...
full textTwo-dimensional gel electrophoresis and immunoblotting of Campylobacter pylori proteins.
Whole-cell, outer-membrane protein, flagellum-associated antigens and partially purified urease of Campylobacter pylori were analyzed by two-dimensional gel electrophoresis. C. pylori strains were readily distinguished from strains of Campylobacter jejuni, C. coli, and C. fetus by absence of major outer membrane proteins with Mrs of 41,000 to 45,000. C. pylori strains also lacked the acidic sur...
full textImproved Immunogenicity of Tetanus Toxoid by Brucella abortus S19 LPS Adjuvant
Background: Adjuvants are used to increase the immunogenicity of new generation vaccines, especially those based on recombinant proteins. Despite immunostimulatory properties, the use of bacterial lipopolysaccharide (LPS) as an adjuvant has been hampered due to its toxicity and pyrogenicity. Brucella abortus LPS is less toxic and has no pyrogenic properties compared to LPS from other gram nega...
full textTwo-dimensional gel electrophoresis and immunoblotting of Campylobacter outer membrane proteins.
We characterized outer membrane proteins (OMPs) from selected Campylobacter jejuni, C. coli, and C. fetus strains by two-dimensional gel electrophoresis (2DGE), using isoelectric focusing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and by immunoblotting with immune rabbit serum. The flagellar band with a molecular mass of 63 kilodaltons (kDa) demonstrated previousl...
full textMy Resources
Journal title
volume 30 issue 1
pages 10- 15
publication date 2005-03-01
By following a journal you will be notified via email when a new issue of this journal is published.
Hosted on Doprax cloud platform doprax.com
copyright © 2015-2023