David A. Relman

Publication Details

  • GENETIC-CHARACTERIZATION OF BORDETELLA-PERTUSSIS FILAMENTOUS HEMAGGLUTININ - A PROTEIN PROCESSED FROM AN UNUSUALLY LARGE PRECURSOR MOLECULAR MICROBIOLOGY Domenighini, M., Relman, D., Capiau, C., FALKOW, S., PRUGNOLA, A., Scarlato, V., Rappuoli, R. 1990; 4 (5): 787-800

    Abstract:

    The nucleotide sequence of the structural gene for filamentous haemagglutinin (FHA), fhaB, a crucial adherence factor for Bordetella pertussis, has been determined. Its 10774 nucleotides are far more than necessary to encode the 220 kD biologically active, mature polypeptide product, suggesting a role for co- or post-translational processing. Fusion proteins derived from various portions of the fhaB open reading frame (ORF) were used to generate polyclonal antisera. Western immunoblot analysis of purified FHA and Bordetella sp. whole cell extracts with these antisera indicated that the 220 kD product is encoded by the 5' portion of the ORF and that the smaller polypeptide species are breakdown products of this polypeptide. These data, as well as N-terminal amino acid sequencing of the major polypeptide species, suggest a scheme for the proteolytic processing of an FHA precursor polypeptide.

    View details for Web of Science ID A1990DF11700011

    View details for PubMedID 2388559

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