Open AccessSpecific binding of lactoferrin to Aeromonas hydrophila
Author(s) -
Kishore A.R.,
Erdei J.,
Naidu S.S.,
Falsen E.,
Forsgren A.,
Naidu A.S.
Publication year - 1991
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1991.tb04399.x
Subject(s) - lactoferrin , aeromonas hydrophila , transferrin , binding site , plasma protein binding , binding protein , chemistry , biochemistry , biology , microbiology and biotechnology , bacteria , gene , genetics
The interaction of lactoferrin (Lf) with Aeromonas hydrophila ( n = 28) was tested in a 125 I‐labeled protein‐binding assay. The mean percent binding values for human Lf (HLf) and bovine Lf (BLf) were 13.4±2.0 (SEM), and 17.5±2.7 (SEM), respectively. The Lf binding was characterized in type strain A. hydrophila subsp. hydrophila CCUG 14551. The HLf and BLf binding reached a complete saturation within 2 h. Unlabeled HLf and BLf displaced 125 I‐HLf binding in a dose‐dependent manner, and more effectively by the heterologous (1 μg for 50% inhibition) than the homologous (10 μg for 50% inhibition) ligand. Apo‐ and holo‐forms of HLf and BLf both inhibited more than 80%, while mucin caused approx. 50% inhibition of the HLf binding. Various other proteins (including transferrin) or carbohydrates did not block the binding. Two HLf‐binding proteins with an estimated molecular masses of 40 kDa and 30 kDa were identified in a boiled‐cell‐envelope preparation, while the unboiled cell envelope demonstrated a short‐ladder pattern at the top of the separating gel and a second band at approx. 60 kDa position. These data establish a specific interaction of Lf and the Lf‐binding proteins seem to be porins in A. hydrophila .