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Infection and Immunity, November 1998, p. 5565-5569, Vol. 66, No. 11
Department of Immunology, Forsyth Dental
Center, Boston, Massachusetts 02115,1 and
Department of Periodontics, College of Dentistry, University
of Illinois at Chicago, Chicago, Illinois
606122
Received 4 May 1998/Returned for modification 8 June 1998/Accepted 20 August 1998
Three purified glucan binding proteins (GBP-2, GBP-3, and
GBP-5) from Streptococcus sobrinus 6715 were compared
structurally by mass spectroscopy of tryptic fragments and
antigenically by Western blot analysis with rat antisera to each GBP or
to peptides containing putative glucan binding epitopes of mutans
streptococcal glucosyltransferases. Structural and antigenic
analyses indicated that GBP-3 and GBP-5 are very similar
but that both are essentially unrelated to GBP-2. None of these
S. sobrinus GBPs appeared to have a strong antigenic
relationship with GBPs from Streptococcus mutans. Thus,
S. sobrinus GBP-2 and GBP-3 appear to be distinct proteins with potentially different functions. S. sobrinus
GBP-5 may be a proteolytic fragment of GBP-3, or,
alternatively, the genes coding for these proteins may be closely
related.
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Structural and Antigenic Characteristics of Streptococcus
sobrinus Glucan Binding Proteins

*
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.
This author has previously published under the name Christine D. Wu-Yuan.
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