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Critical Reviews in Oral Biology & Medicine
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4(3):315-323 (1993)     Crit Rev Oral Biol Med
© 1993 SAGE Publications

Low-Molecular-Mass Human Salivary Mucin, MG2: Structure and Binding of Pseudomonas aeruginosa

Molakala S. Reddy

Department of Oral Biology and Dental Research Institute, School of Dental Medicine, State University of New York at Buffalo, Buffalo, NY 14214

Michael J. Levine

Department of Oral Biology and Dental Research Institute, School of Dental Medicine, State University of New York at Buffalo, Buffalo, NY 14214

William Paranchych

Department of Microbiology, University of Alberta, Edmonton, Alberta, T6G 2E9, Canada

Low-molcular-mass human salivary mucin, MG2, was isolated from human submandibular-sublingual saliva (HSMSL) employing citraconylation, gel filtration, and ion-exchange chromatography. Following proteolysis with trypsin, two glycopeptides were purified. The higher molecular weight glycopeptide was highly glycosylated with O-linked units. The lower molecular weight glycopeptide was less glycosylated and contained most of the N-linked units. Interaction between components of HSMSL and pili of Pseudomonas aeruginosa was examined by an overlay binding assay. Pili were found to bind to MG2. Preliminary studies indicated that the binding may involve a protein to protein interaction.

Key Words: mucin • glycoprotein • saliva • Pseudomonas aeruginosa.

Critical Reviews in Oral Biology & Medicine, Vol. 4, No. 3, 315-323 (1993)
DOI: 10.1177/10454411930040030901
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