Open AccessInhibition of Bordetella pertussis filamentous hemagglutinin‐mediated cell adherence with monoclonal antibodies
Author(s) -
Leininger Elizabeth,
Probst Peter G.,
Brennan Michael J.,
Kenimer James G.
Publication year - 1993
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.1574-6968.1993.tb05931.x
Subject(s) - filamentous haemagglutinin adhesin , monoclonal antibody , bordetella pertussis , hemagglutinin (influenza) , epitope , pertactin , pertussis toxin , bacterial adhesin , microbiology and biotechnology , biology , chinese hamster ovary cell , bordetella , agglutination (biology) , antibody , western blot , virology , cell culture , bacteria , biochemistry , g protein , escherichia coli , immunology , receptor , genetics , gene
Filamentous hemagglutinin (FHA), a 220‐kDa protein located on the surface of Bordetella pertussis , is one of the major cell adhesins of this bacterium. We have produced three hybridoma cell lines that express monoclonal antibodies (mAbs) against FHA: X3C, X3E and X4B. The anti‐FHA mAbs X3C and X3E reacted with 220‐kDa FHA protein bands on Western blots. The mAb X4B, which reacted with FHA in ELISA, did not bind to FHA in a Western blot assay. All three mAbs seemed to be directed to the same epitope or to epitopes in close proximity as suggested by competition ELISAs. All three mAbs were able to inhibit the adherence of Chinese hamster ovary cells to purified FHA, and they could also inhibit the FHA‐mediated agglutination of goose red blood cells. The attachment of B. pertussis to epithelial cell monolayers was inhibited by the mAb X3C. These antibodies are very useful probes to identify the presence of FHA in bordetellae species and in clinical reagents such as pertussis vaccines, and to characterize the functional domains of this important bacterial adhesin.