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Journal of Bacteriology, August 1999, p. 4834-4841, Vol. 181, No. 16
Department of Microbiology, Technical
University of Denmark, DK-2800 Lyngby, Denmark,1
and Institute of Medical Microbiology,
Justus-Liebig-Universität, D-35392 Giessen,
Germany2
Received 1 April 1999/Accepted 4 June 1999
Antigen 43 (Ag43), the product of the flu gene, is a
surface-displayed autotransporter protein of Escherichia
coli. Ag43 is responsible for the autoaggregation and
flocculation of static liquid cultures of many E. coli
strains. The expression of Ag43 has been reported to be phase variable
and controlled by the product of the oxyR gene. Type 1 fimbriae are thin adhesive thread-like surface organelles responsible
for bacterial receptor recognition and tissue colonization. Like that
of Ag43, the expression of type 1 fimbriae is phase variable.
Interestingly, previous results have suggested that the expression of
type 1 fimbriae and the expression of Ag43 are mutually exclusive. In
the present report, we show, by use of well-defined mutants, that
fimbriation abolishes Ag43-mediated autoaggregation but does not affect
Ag43 expression. Autoaggregation is shown to require an intercellular
Ag43-Ag43 interaction, and the physical presence of fimbriae on the
cells seems to abrogate this interaction. The Ag43 or OxyR status does not appear to influence fimbria expression, and our results suggest that the expression of Ag43 and the expression of fimbriae are independent processes.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Antigen-43-Mediated Autoaggregation of
Escherichia coli Is Blocked by Fimbriation
*
Corresponding author. Mailing address: Department of
Microbiology, Bldg. 301, Technical University of Denmark, DK-2800
Lyngby, Denmark. Phone: 45 45 25 2506. Fax: 45 45 93 28 09. E-mail:
impk{at}pop.dtu.dk.
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