Title: Conserved regions in the sequence of the F4 (K88) fimbrial adhesin FaeG suggest a donor strand mechanism in F4 assembly
Authors: Verdonck, F ×
Cox, E
Schepers, E
Imberechts, H
Joensuu, J
Goddeeris, Bruno #
Issue Date: Sep-2004
Publisher: Elsevier science bv
Series Title: Veterinary microbiology vol:102 issue:3-4 pages:215-225
Abstract: Oral immunization of newly weaned piglets with recombinant F4 (K88) fimbrial adhesin FaeG induces a F4-specific immune response, significantly reducing F4(+) Escherichia coli excretion following challenge. In order to use FaeG subunits in an Oral vaccine against F4(+) enterotoxigenic E. coli, it is necessary to determine the conservation of the adhesin subunit. Hereto, the faeG sequence was determined of 21 F4ac(+) E. coli field isolates from piglets with diarrhoea and subsequently compared with these of the reference strain GIS26 and previously reported FaeG sequences from F4ab, F4ac and F4ad antigenic variant strains. The FaeG amino acid sequence was 96-100% homologous within each F4 serotype, but only 92 and 88% when the F4ab and F4ad antigenic variants were compared with the F4ac antigenic variant. Furthermore, the conserved regions of the adhesin suggest a donor strand mechanism in F4 fimbriae assembly as reported for type 1 and P pili. In conclusion, the results of the reported experiments support the usefulness FaeG in an oral subunit vaccine against F4(+) E. coli infections or as a mucosal carrier since the adhesin is conserved among F4(+) E coli field isolates. (C) 2004 Elsevier B.V. All rights reserved.
ISSN: 0378-1135
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Division of Gene Technology (-)
× corresponding author
# (joint) last author

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