C. Carnoy et al., ALTERED CARBOHYDRATE-COMPOSITION OF SALIVARY MUCINS FROM PATIENTS WITH CYSTIC-FIBROSIS AND THE ADHESION OF PSEUDOMONAS-AERUGINOSA, American journal of respiratory cell and molecular biology, 9(3), 1993, pp. 323-334
We compared the chemical composition of salivary mucin glycopeptides f
rom cystic fibrosis (CF) and from non-CF subjects and the adhesion of
Pseudomonas aeruginosa to these different salivary glycopeptides. Thre
e pools of CF saliva, four pools of non-CF saliva, one individual CF s
aliva, and one individual non-CF saliva were studied. The soluble frac
tion of the saliva was treated with pronase, and gel filtration was pe
rformed to obtain high and low molecular mass salivary mucin glycopept
ides. The yield of total glycopeptides was significantly higher from C
F than from non-CF saliva. Furthermore, the chemical composition revea
led a significantly higher sialic acid content in CF than in non-CF mu
cin glycopeptides, and higher sulfate and fucose content in CF than in
non-CF high molecular mass glycopeptides. We studied the adhesion of
a nonmucoid strain of P. aeruginosa (1244), its nonpiliated isogenic d
erivative, and a mucoid strain (M35) to salivary mucin glycopeptides f
rom patients with CF and from non-CF subjects. The three strains bound
significantly more to the CF salivary glycopeptides than to the corre
sponding non-CF salivary glycopeptides. The nonpiliated isogenic mutan
t of P. aeruginosa 1244 also bound to CF salivary glycopeptides, sugge
sting that the adhesion of P. aeruginosa could involve nonpilus adhesi
ns. Furthermore, neuraminidase treatment of CF glycopeptides decreased
the adhesion of P aeruginosa 1244. Altogether these results suggested
that differences in mucins may in part explain the specificity of P a
eruginosa for CF.