Open AccessMonoclonal antibodies against the FhuA (TonA) protein of the Escherichia coli outer membrane
Author(s) -
Dimoudis Nikolaos,
Komischke Klemens,
Braun Volkmar
Publication year - 1984
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.1574-6968.1984.tb01383.x
Subject(s) - colicin , monoclonal antibody , ferrichrome , escherichia coli , biology , antibody , bacterial outer membrane , microbiology and biotechnology , affinity chromatography , biochemistry , gene , enzyme , immunology
Outer membranes of Escherichia coli K‐12 were used to isolate hybridoma cell lines that produce monoclonal antibodies against the FhuA (TonA) protein. Two monoclonal antibodies were obtained from independent immunization and fusion experiments. The antibodies belonged to the subclass IgG 1 and κ, and IgG 2b and κ, respectively. The latter antibody was purified by affinity chromatography on protein A‐Sepharose. The culture supernatants of the hybridoma cell lines and the isolated antibody inhibited adsorption of the phages T5 and T1 to E. coli cells while binding of phage ø80, which also uses the FhuA protein as a receptor, remained unaffected. The specificity of the antibodies to the FhuA protein was supported by the prevention of killing of cells by colicin M and by the lack of inhibition of colicin B and of phage BG23. Transport of iron(III) as ferrichrome complex was not inhibited by the isolated antibody. However, partial competition with the adsorption of the phages T2, TuIb and T6 was observed which may indicate an organization of certain functional phage receptors into clusters.