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