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Originally published In Press as doi:10.1074/jbc.M203788200 on June 5, 2002

J. Biol. Chem., Vol. 277, Issue 35, 32109-32115, August 30, 2002
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Identification of the Bacteria-binding Peptide Domain on Salivary Agglutinin (gp-340/DMBT1), a Member of the Scavenger Receptor Cysteine-rich Superfamily*

Floris J. BikkerDagger §, Antoon J. M. LigtenbergDagger , Kamran NazmiDagger , Enno C. I. VeermanDagger , Wim van't HofDagger , Jan G. M. BolscherDagger , Annemarie Poustka, Arie V. Nieuw AmerongenDagger , and Jan Mollenhauer

From the Dagger  Department of Dental Basic Sciences, Section of Oral Biochemistry, Academic Centre for Dentistry Amsterdam (ACTA), 1081 BT Amsterdam, The Netherlands and the  Division of Molecular Genome Analysis, Deutsches Krebsforschungszentrum (DKFZ), D-69120 Heidelberg, Germany

Salivary agglutinin is encoded by DMBT1 and identical to gp-340, a member of the scavenger receptor cysteine-rich (SRCR) superfamily. Salivary agglutinin/DMBT1 is known for its Streptococcus mutans agglutinating properties. This 300-400 kDa glycoprotein is composed of conserved peptide motifs: 14 SRCR domains that are separated by SRCR-interspersed domains (SIDs), 2 CUB (C1r/C1s Uegf Bmp1) domains, and a zona pellucida domain. We have searched for the peptide domains of agglutinin/DMBT1 responsible for bacteria binding. Digestion with endoproteinase Lys-C resulted in a protein fragment containing exclusively SRCR and SID domains that binds to S. mutans. To define more closely the S. mutans-binding domain, consensus-based peptides of the SRCR domains and SIDs were designed and synthesized. Only one of the SRCR peptides, designated SRCRP2, and none of the SID peptides bound to S. mutans. Strikingly, this peptide was also able to induce agglutination of S. mutans and a number of other bacteria. The repeated presence of this peptide in the native molecule endows agglutinin/DMBT1 with a general bacterial binding feature with a multivalent character. Moreover, our studies demonstrate for the first time that the polymorphic SRCR domains of salivary agglutinin/DMBT1 mediate ligand interactions.

* This study was financially supported by The Netherlands Interuniversity Research School of Dentistry (IOT), the Deutsche Krebshilfe Grant 10-1835-Mo1 (to J. M.), and the Wilhelm Sander-Stiftung Grant 99.018.1 (to A. P.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands. Tel.: 0031-(0)20-444- 8674; Fax: 0031-(0)20-444-8685; E-mail: fj.bikker.obc.acta@med.vu.nl.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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