Open AccessInteraction of the Bordetella pertussis filamentous hemagglutinin with heparin
Author(s) -
Menozzi Franco D.,
Gantiez Claudie,
Locht Camille
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.tb04417.x
Subject(s) - filamentous haemagglutinin adhesin , bordetella pertussis , heparin , microbiology and biotechnology , hemagglutinin (influenza) , bacterial adhesin , bordetella , pertussis toxin , hemagglutination , chemistry , biology , biochemistry , escherichia coli , bacteria , antigen , immunology , receptor , g protein , gene , genetics
Summary Heparin, a glycosaminoglycan synthesized in connective tissue‐mast cells, appeared to inhibit the hemagglutination of rabbit erythrocytes induced by the filamentous hemagglutinin (FHA), a major adhesin of Bordetella pertussis . This inhibition suggested an interaction of heparin with the FHA region responsible for the hemagglutination activity. FHA‐heparin interactions may play a role in bacterial attachment and persistence in the lungs during human pertussis. To confirm a direct FHA‐heparin interaction, heparin was used as ligand in an affinity chromatography procedure. This technique allowed to purify FHA directly from the bacterial culture medium in a single‐step using heparin‐Sepharose CL‐6B or Zetaffinity heparin 60 disks. The purified FHA was highly immunoreactive with anti‐FHA monoclonal anti‐bodies and showed no signs of degradation after 15 successive cycles of freezing‐thawing. The described purification method is simple, and suitable for the rapid preparation of FHA.