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Genetic characterization of Bordetella pertussis filamentous haemagglutinin: a protein processed from an unusually large precursor
Author(s) -
Domenighini M.,
Relman D.,
Capiau C.,
Falkow S.,
Prugnola A.,
Scarlato V.,
Rappuoli R.
Publication year - 1990
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1990.tb00649.x
Subject(s) - bordetella pertussis , biology , open reading frame , polyclonal antibodies , antiserum , bordetella , nucleic acid sequence , peptide sequence , gene product , amino acid , microbiology and biotechnology , fusion protein , biochemistry , gene , recombinant dna , antigen , bacteria , genetics , gene expression
Summary The nucleotide sequence of the structural gene for filamentous haemagglutinin (FHA), fhaB , a crucial adherence factor for Bordetella perfussis , has been determined. Its 10774 nucleotides are far more than necessary to encode the 220kD 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 220kD 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.