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Infection and Immunity, May 1999, p. 2638-2642, Vol. 67, No. 5
Department of Immunology, Forsyth Dental
Center, Boston, Massachusetts 02115
Received 3 December 1998/Returned for modification 8 January
1999/Accepted 3 February 1999
We examined the immunogenicity and induction of inhibitory activity
of 19-mer synthetic peptides which contained putative catalytic regions
that were associated with the
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Antibody to Glucosyltransferase Induced by
Synthetic Peptides Associated with Catalytic Regions of
-Amylases
5 (EAW) and
7 (HDS) strand elements of the suggested
(
,
)8 catalytic barrel domain of Streptococcus
mutans glucosyltransferase (GTF). Both peptides readily induced
serum immunoglobulin G (IgG) and salivary IgA antipeptide activity
which was reactive both with the inciting peptide and with intact
S. mutans GTF. Antisera to each peptide construct also
inhibited the ability of S. mutans GTF to synthesize glucan. These observations support the existence of catalytic subdomains containing glutamate and tryptophan (EAW) or aspartate and
histidine (HDS) residues, each of which have been suggested to be
involved with the catalytic activity of GTF. Furthermore, the epitopes
defined in these sequences have significant immunogenicity and can
induce immune responses which interfere with GTF-mediated glucan synthesis.
*
Corresponding author. Mailing address: Department of
Immunology, Forsyth Dental Center, 140 The Fenway, Boston, MA 02115. Phone: (617) 262-5200, ext. 309. Fax: (617) 262-4021. E-mail: dsmith{at}forsyth.org.
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