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Journal of Clinical Microbiology, March 2001, p. 1178-1183, Vol. 39, No. 3
0095-1137/01/$04.00+0   DOI: 10.1128/JCM.39.3.1178-1183.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Molecular Characterization of fliD Gene Encoding Flagellar Cap and Its Expression among Clostridium difficile Isolates from Different Serogroups

Albert Tasteyre,1 Tuomo Karjalainen,1 Véronique Avesani,2 Michel Delmée,2 Anne Collignon,1 Pierre Bourlioux,1 and Marie-Claude Barc1,*

Faculté de Pharmacie, Département de Microbiologie, Université de Paris-Sud, 92296 Châtenay-Malabry Cedex, France,1 and Unité de Microbiologie, Département de Biologie, Université Catholique de Louvain, 1200 Brussels, Belgium2

Received 7 September 2000/Returned for modification 1 December 2000/Accepted 19 December 2000

The fliD gene encoding the flagellar cap protein (FliD) of Clostridium difficile was studied in 46 isolates belonging to serogroups A, B, C, D, F, G, H, I, K, X, and S3, including 30 flagellated strains and 16 nonflagellated strains. In all but three isolates, amplification by PCR and reverse transcription-PCR demonstrated that the fliD gene is present and transcribed in both flagellated and nonflagellated strains. PCR-restriction fragment length polymorphism (RFLP) analysis of amplified fliD gene products revealed interstrain homogeneity, with one of two major patterns (a and b) found in all but one of the strains, which had pattern c. A polyclonal monospecific antiserum raised to the recombinant FliD protein reacted in immunoblots with crude flagellar preparations from 28 of 30 flagellated strains but did not recognize FliD from nonflagellated strains. The fliD genes from five strains representative of the three different RFLP groups were sequenced, and sequencing revealed 100% identity between the strains with the same pattern and 88% identity among strains with different patterns. Our results show that even though FliD is a structure exposed to the outer environment, the flagellar cap protein is very well conserved, and this high degree of conservation suggests that it has a very specific function in attachment to cell or mucus receptors.

* Corresponding author. Mailing address: Faculté de Pharmacie, Département de Microbiologie. Université de Paris-Sud, 5, rue J. B. Clément, 92296 Châtenay-Malabry Cedex. France. Phone: (33)-1 46 83 55 49. Fax: (33)-1 46 83 58 83. E-mail: marie-claude.barc{at}cep.u-psud.fr.

Journal of Clinical Microbiology, March 2001, p. 1178-1183, Vol. 39, No. 3
0095-1137/01/$04.00+0   DOI: 10.1128/JCM.39.3.1178-1183.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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