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Localization of purified surface molecules (lipopolysaccharide and A‐protein) from Aeromonas salmonicida in the kidney and spleen from Atlantic salmon, Salmo salar L.
Author(s) -
Stensvåg K.,
Arnesen S. M.,
Bøgwald J.,
Jørgensen T. Ò.
Publication year - 1999
Publication title -
journal of fish diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.819
H-Index - 85
eISSN - 1365-2761
pISSN - 0140-7775
DOI - 10.1046/j.1365-2761.1999.00174.x
Subject(s) - aeromonas salmonicida , salmo , biology , spleen , lipopolysaccharide , fishery , kidney , microbiology and biotechnology , fish <actinopterygii> , zoology , immunology , genetics
Lipopolysaccharide (LPS) and A‐layer protein purified from Aeromonas salmonicida were administered intravenously in Atlantic salmon, Salmo salar L., either alone or in combination. Tissues from each organ were examined by immunohistochemical techniques, using a polyclonal antiserum against A‐protein and a monoclonal antibody against LPS. When given simultaneously, the antigens seemed to be taken up by different cells in both the head and trunk kidney. The most striking finding was that A‐protein was located in epithelial cells in renal proximal tubules, in contrast to LPS, which was not detected in this location. The amount of A‐protein in the tissue increased with time until 2 h after injection. Autoradiography of SDS polyacrylamide gel electrophoresis of head kidney homogenates showed that in vivo processing of A‐protein coupled to iodinated tyramine cellobiose ( 125 I‐TC‐A‐protein) was completed within 24 h, in contrast to LPS, which was maintained in tissues. The findings of the present study suggest that cells of the head kidney of Atlantic salmon are capable of taking up and processing the A‐protein.