Critical Reviews in Oral Biology & Medicine, Vol 4, 315-323, Copyright © 1993 by International & American Associations for Dental Research
Low-molecular-mass human salivary mucin, MG2: structure and binding of Pseudomonas aeruginosa
M. S. Reddy, M. J. Levine and W. Paranchych
Department of Oral Biology, School of Dental Medicine, State University of New York, Buffalo 14214.
Low-molecular-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.
