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Originally published In Press as doi:10.1074/jbc.M006928200 on September 27, 2000

J. Biol. Chem., Vol. 275, Issue 51, 39860-39866, December 22, 2000
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Salivary Agglutinin, Which Binds Streptococcus mutans and Helicobacter pylori, Is the Lung Scavenger Receptor Cysteine-rich Protein gp-340*

Akraporn Prakobpholab, Feng Xubc, Van M. Hoangbd, Thomas Larssone, Jorgen Bergstrome, Ingegerd Johanssonc, Lars Frängsmyrc, Uffe Holmskovf, Hakon Lefflerg, Christina Nilssonc, Thomas Borénc, Jo Rae Wrighth, Nicklas Strömbergbc, and Susan J. Fisherabdijk

From the Departments of a Stomatology, i Anatomy, d Pharmaceutical Chemistry, and j Obstetrics, Gynecology, and Reproductive Sciences, University of California, San Francisco, California 94143, the c Department of Odontology/Cariology and Oral Microbiology, Umeå University, SE-901 87 Umeå, Sweden, the f Department of Medical Microbiology, Institute of Medical Biology, University of Odense, DK-5000 Odense C, Denmark, the e Department of Medical Biochemistry, University of Göteborg, SE-413 90 Göteborg, Sweden, the g Department of Molecular Medicine, Lund University, SE-221 00 Lund, Sweden, and the h Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710

Salivary agglutinin is a high molecular mass component of human saliva that binds Streptococcus mutans, an oral bacterium implicated in dental caries. To study its protein sequence, we isolated the agglutinin from human parotid saliva. After trypsin digestion, a portion was analyzed by matrix-assisted laser/desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS), which gave the molecular mass of 14 unique peptides. The remainder of the digest was subjected to high performance liquid chromatography, and the separated peptides were analyzed by MALDI-TOF/post-source decay; the spectra gave the sequences of five peptides. The molecular mass and peptide sequence information showed that salivary agglutinin peptides were identical to sequences in lung (lavage) gp-340, a member of the scavenger receptor cysteine-rich protein family. Immunoblotting with antibodies that specifically recognized either lung gp-340 or the agglutinin confirmed that the salivary agglutinin was gp-340. Immunoblotting with an antibody specific to the sialyl Lex carbohydrate epitope detected expression on the salivary but not the lung glycoprotein, possible evidence of different glycoforms. The salivary agglutinin also interacted with Helicobacter pylori, implicated in gastritis and peptic ulcer disease, Streptococcus agalactiae, implicated in neonatal meningitis, and several oral commensal streptococci. These results identify the salivary agglutinin as gp-340 and suggest it binds bacteria that are important determinants of either the oral ecology or systemic diseases.

* This work was supported by National Institutes of Health Grants DE 07244, HL 51134, and RR 01614, Swedish Medical Research Council Grants 10435, 12165, 10906, and 11218, and the Swedish Foundation for Strategic Research.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.

b This paper is an equal contribution of two research groups with two senior authors (S. J. F. and N. S.) and three first authors (A. P., F. X., and V. M. H.).

k To whom correspondence should be addressed: HSW 604, University of California, San Francisco, CA 94143-0512. Tel.: 415-476-5297; Fax: 415-476-4204; E-mail: sfisher@cgl.ucsf.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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