Filamentous hemagglutinin of Bordetella pertussis: nucleotide sequence and crucial role in adherence.

• DOI: 10.1073/pnas.86.8.2637
• Publication Date: 2006-05-31T11:17:06Z
• Authors: D A Relman; M Domenighini; E Tuomanen; R Rappuoli; S Falkow
• Keywords: 0301 basic medicine; Base Sequence; Molecular Sequence Data; Respiratory System; In Vitro Techniques; Regulatory Sequences, Nucleic Acid; Bacterial Adhesion; Bordetella pertussis; Cell Line; 3. Good health; 03 medical and health sciences; Hemagglutinins; Genes, Bacterial; Cricetinae; Antigens, Surface; Animals; Amino Acid Sequence; Cloning, Molecular; Cell Adhesion Molecules

Filamentous hemagglutinin is a surface-associated adherence protein of Bordetella pertussis, which is a component of some new acellular pertussis vaccines. The nucleotide sequence of an open reading frame that encompasses the filamentous hemagglutinin structural gene, fhaB, suggests that proteolytic processing is necessary to generate the mature 220-kDa filamentous hemagglutinin product. An Arg-Gly-Asp (RGD) tripeptide is found within filamentous hemagglutinin that may be involved in its adherence properties. An internal in-frame deletion in fhaB, encompassing the RGD region, causes loss of B. pertussis-binding to ciliated eukaryotic cells, confirming a potential role for this protein in host-cell binding and infection.