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Infection and Immunity, November 1999, p. 5755-5761, Vol. 67, No. 11
Department of Pathobiology, School of
Veterinary Medicine, University of Pennsylvania, Philadelphia,
Pennsylvania 19104
Received 3 May 1999/Returned for modification 7 July 1999/Accepted 26 August 1999
The FasG subunit of the 987P fimbriae of enterotoxigenic strains of
Escherichia coli was previously shown to mediate fimbrial binding to a glycoprotein and a sulfatide receptor on intestinal brush
borders of piglets. Moreover, the 987P adhesin FasG is required for
fimbrial expression, since fasG null mutants are
nonfimbriated. In this study, fasG was modified by
site-directed mutagenesis to study its sulfatide binding properties.
Twenty single mutants were generated by replacing positively charged
lysine (K) or arginine (R) residues with small, nonpolar alanine (A)
residues. Reduced levels of binding to sulfatide-containing liposomes
correlated with reduced fimbriation and FasG surface display in four
fasG mutants (R27A, R286A, R226A, and R368). Among the 16 remaining normally fimbriated mutants with wild-type levels of
surface-exposed FasG, only one mutant (K117A) did not interact at all
with sulfatide-containing liposomes. Four mutants (K117A, R116A, K118A,
and R200A) demonstrated reduced binding to such liposomes. Since
complete phenotypic dissociation between the structure and specific
function of 987P was observed only with mutant K117A, this residue is
proposed to play an essential role in the FasG-sulfatide interaction,
possibly communicating with the sulfate group of sulfatide by hydrogen
bonding and/or salt bridge formation. Residues K17, R116, K118, and
R200 may stabilize this interaction.
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Lysine Residue 117 of the FasG Adhesin of
Enterotoxigenic Escherichia coli Is Essential for Binding
of 987P Fimbriae to Sulfatide
*
Corresponding author. Mailing address: University of
Pennsylvania School of Veterinary Medicine, 3800 Spruce St.,
Philadelphia, PA 19104-6049. Phone: (215) 898-1695. Fax: (215)
898-7887. E-mail: dmschiff{at}vet.upenn.edu.
Infection and Immunity, November 1999, p. 5755-5761, Vol. 67, No. 11
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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