Autor: |
Bjørnsdott1r, R., Eggset, G., Nilsen, R., Jørgensen, T. ø. |
Předmět: |
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Zdroj: |
Journal of Fish Diseases; Mar1992, Vol. 15 Issue 2, p105-118, 14p |
Abstrakt: |
The predominant cell surface protein (A-protein) of Aeromonas salmonicida has been purified by a method utilizing a glycine/hydroehloride extraction from whole cells and HPLC/ion exchanger (DEAE) columns. This procedure yielded two LPS-free molecules (a 40- and a 50-kDa form) both shown to contain A-protein determinants. The former appears to be a digest product of the latter, as a serine protease produced by A. salmonicida was shown to process the 50-kDa form into a 40-kDa molecule in vitro. The A-layer protein was shown to contain one isoform, although multiple isoelectric forms appeared as preparative artifacts, probably due to deamidation. The A-layer protein and LPS are the most significant surface antigens recognized by the Atlantic salmon B-lymphocytes or antibodies. Immunological studies of LPS-free and LPS-containing A-protein preparations were undertaken to test whether the two components behave like antigenic competitors or whether the LPS moiety could adjuvant the antibody response against the A-protein. The latter was shown to be the case. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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