The A‐layer protein of Aeromonas salmonicida: further characterization and a new isolation procedure
Abstract. The predominant cell surface protein (A‐protein) of Aeromonas salmonicida has been purified by a method utilizing a glycine/hydrochloridc extraction from whole cells and HPLC/ion exchanger (DEAE) columns. This procedure yielded two LPS‐frec molecules (a 40‐ and a 50‐kDa form) both shown to...
| Published in: | Journal of Fish Diseases |
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| Main Authors: | , , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
1992
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1111/j.1365-2761.1992.tb00645.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1365-2761.1992.tb00645.x https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1365-2761.1992.tb00645.x |
| Summary: | Abstract. The predominant cell surface protein (A‐protein) of Aeromonas salmonicida has been purified by a method utilizing a glycine/hydrochloridc extraction from whole cells and HPLC/ion exchanger (DEAE) columns. This procedure yielded two LPS‐frec 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 arc 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 antigenie competitors or whether the LPS moiety could adjuvant the antibody response against the A‐protein. The latter was shown to be the case. |
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