HumanSalivary Mucin, MG2: Structure andBinding ofPseudomonas aeruginosa

Low-molcular-mass humansalivary mucin, MG2,was isolated fromhumansubmandibular-sublingual saliva (HSMSL)employing citraconylation, gelfiltration, andion-exchange chromatography. Following proteolysis withtrypsin, two glycopeptides werepurified. Thehigher molecular weight glycopeptide washighly glycosylated with0-linked units. Thelower molecular weight glycopeptide wasless glycosylated andcontained mostoftheN-linked units. Interaction between components ofHSMSLandpili ofPseudomonas aeruginosa was examined byanoverlay binding assay.Pili werefound tobindtoMG2. Preliminary studies indicated thatthebinding may involve aprotein toprotein interaction.