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Bulletin No. 20 - Winter 2004
BacterologyEscherichia coli & Clostridium dificile / perfrigens
VERDONCK F, COX E, SCHEPERS E, IMBERECHTS H, JOENSUU J, GODDEERIS BM
Conserved regions in the sequence of the F4 (K88) fimbrial adhesin FaeG suggest a donor strand mechanism in F4 assembly.
Veterinary Microbiology, 2004, Volume 102, N?º3-4, 215-225
The amino acid sequence of the FaeG subunit of adhesin F4 was determined in 21 enterotoxigenic Escherichia coli (ETEC) field strains isolated from piglets with diarrhea. In this study, the conservation of such FaeG sequence which showed a 96-100% homology was clearly demonstrated. Moreover, due to the position and aminoacid sequence of some very conserved motifs, a donor strand mechanism in F4 assembly was hypothesized. These results indicate that it would be of great interest understanding whether the FaeG sequence could be used to design a mucosal subunit vaccine against F4+ ETEC infections.
