The central, surface-exposed region of the flagellar hook protein FlgE of Campylobacter jejuni shows hypervariability among strains

• Published in: Journal of bacteriology Vol. 180; no. 14; pp. 3711 - 3714
• Main Authors: Lüneberg, E, Glenn-Calvo, E, Hartmann, M, Bär, W, Frosch, M
• Format: Journal Article
• Language: English
• Published: United States American Society for Microbiology 01.07.1998
• Series: Note
• Subjects: Amino Acid Sequence; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - immunology; Campylobacter jejuni - genetics; Campylobacter jejuni - immunology; Epitopes - immunology; Flagella - genetics; Flagella - immunology; Molecular Sequence Data; Physiology and Metabolism; Sequence Alignment; Sequence Homology, Amino Acid
• ISSN: 0021-9193; 1098-5530
• DOI: 10.1128/jb.180.14.3711-3714.1998

In a previous study, we observed that monoclonal antibodies raised against the hook protein FlgE of Campylobacter jejuni LIO 36, isolate 5226, bound exclusively to this strain. The aim of this study was to elucidate the molecular basis for these binding specificities. The hook protein-encoding gene flgE of C. jejuni was cloned in Escherichia coli and sequenced. The flgE genes of four additional C. jejuni strains were amplified by PCR and also sequenced. Comparison of the deduced amino acid sequences revealed a high degree of variability in the central parts of the FlgE proteins among the strains, including variable and hypervariable domains. These findings may indicate a selective pressure of C. jejuni hosts, forcing the bacteria to generate variations in surface-exposed antigenic determinants.