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. Copyright © 1990, Wiley Blackwell. All rights reserved
Domenighini M., Relman D., Capiau C., Falkow S., Prugnola A., Scarlato V., et al. (1990). Genetic characterization of Bordetella pertussis filamentous haemagglutinin: a protein processed from an unusually large precursor. MOLECULAR MICROBIOLOGY, 4(5), 787-800 [10.1111/j.1365-2958.1990.tb00649.x].
Genetic characterization of Bordetella pertussis filamentous haemagglutinin: a protein processed from an unusually large precursor
Scarlato V.;
1990
Abstract
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. Copyright © 1990, Wiley Blackwell. All rights reservedI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.