CHARACTERIZATION OF A RECOMBINANT FRAGMENT THAT CONTAINS A CARBOHYDRATE-RECOGNITION DOMAIN OF THE FILAMENTOUS HEMAGGLUTININ

The filamentous hemagglutinin (FHA) of Bordetella pertussis plays an i mportant role in establishing infection by attaching the bacteria to t he ciliated respiratory epithelial cells, Expression of DNA encoding r esidues 1141 to 1279 of FHA in Escherichia coli yields a protein of 18 ,000 Da that exhibits some of the carbohydrate recognition properties of FHA (S. M. Prasad, Y. Yin, E. Rodzinski, E. I. Tuomanen, and H. R. Masure, Infect, Immun, 61:2780-2785, 1993). We have constructed an E. coli strain that expresses this protein, designated fragment A, in a s oluble form at markedly elevated levels, Fragment A could be purified, vith high purity and yields and was immunogenic in mice. Both fragment A and anti-fragment A sera inhibited the binding of B. pertussis to a sialo-GM, and to rabbit ciliated cells. These observations demonstrate that this fragment of FHA contains a cellular binding domain capable of eliciting functional antibodies.