Open AccessAntibodies produced against a fragment of filamentous haemagglutinin (FHA) of Bordetella pertussis are able to inhibit hemagglutination induced by the whole adhesin
Author(s) -
Colombi Débora,
Horton Denise S.P.Q.,
Oliveira Maria Leonor S.,
Sakauchi Maria Aparecida,
Ho Paulo L.
Publication year - 2004
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 - 10.1016/j.femsle.2004.09.009
Subject(s) - filamentous haemagglutinin adhesin , bacterial adhesin , hemagglutinin (influenza) , polyclonal antibodies , recombinant dna , biology , hemagglutination , microbiology and biotechnology , antibody , western blot , escherichia coli , virology , biochemistry , gene , receptor , g protein , immunology , pertussis toxin
Filamentous hemagglutinin adhesin (FHA) is important for the adherence of Bordetella pertussis to the host ciliary epithelial cells of the respiratory tract. Several binding domains have been characterized in the FHA molecule. For example, an putative heparin‐binding domain of FHA was previously located in the FHA 442–863 region. In this work, the HEP fragment, corresponding to FHA 430–873 was amplified by PCR and subcloned in an Escherichia coli expression plasmid. Purified recombinant HEP was used to produce polyclonal antibodies in mice that were able to recognize HEP and FHA in ELISA and in Western‐blot assays. Although recombinant HEP displayed low ability to bind heparin and no hemagglutination activity, the anti‐HEP antibodies were able to inhibit FHA mediated hemagglutination activity in goose erythrocytes. These results indicate that other amino acid residues that are not present in the FHA 430–873 fragment may be necessary for heparin binding. Further studies to address the immunogenic response against HEP are also required.