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Journal of Bacteriology, February 2000, p. 728-733, Vol. 182, No. 3
Department of Microbiology, Immunology, and
Molecular Genetics, Albany Medical College, Albany, New York 12208
Received 6 August 1999/Accepted 5 November 1999
Streptococcus mutans glucan-binding protein A (GbpA)
has sequence similarity in its carboxyl-terminal domain with
glucosyltransferases (GTFs), the enzymes responsible for catalyzing the
synthesis of the glucans to which GbpA and GTFs can bind and which
promote S. mutans attachment to and accumulation on the
tooth surface. It was predicted that this C-terminal region, comprised
of what have been termed YG repeats, represents the GbpA glucan-binding domain (GBD). In an effort to test this hypothesis and to quantitate the ligand-binding specificities of the GbpA GBD, several fusion proteins were generated and tested by affinity electrophoresis or by
precipitation of protein-ligand complexes, allowing the determination
of binding constants. It was determined that the 16 YG repeats in GbpA
comprise its GBD and that GbpA has a greater affinity for dextran (a
water-soluble form of glucan) than for mutan (a water-insoluble form of
glucan). Placement of the GBD at the carboxyl terminus was necessary
for maximum glucan binding, and deletion of as few as two YG repeats
from either end of the GBD reduced the affinity for dextran by over
10-fold. Interestingly, the binding constant of GbpA for dextran was
34-fold higher than that calculated for the GBDs of two S. mutans GTFs, one of which catalyzes the synthesis of
water-soluble glucan and the other of which catalyzes the synthesis of
water-insoluble glucan.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Ligand-Binding Properties of the Carboxyl-Terminal Repeat
Domain of Streptococcus mutans Glucan-Binding Protein
A
and
*
Corresponding author. Mailing address: Albany Medical
College, MC-68, 47 New Scotland Ave., Albany, NY 12208. Phone: (518) 262-6286. Fax: (518) 262-5748. E-mail: BanasJ{at}mail.amc.edu.
Present address: Department of Microbiology and Immunology,
University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104.
Journal of Bacteriology, February 2000, p. 728-733, Vol. 182, No. 3
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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