Evidence of lectin-mediated adherence of Moraxella catarrhalis.

Clinical isolates of Moraxella catarrhalis (n = 86) were evaluated for their haemagglutinating activity with different types of erythrocytes. Of all the isolates tested, 12 did not agglutinate with any of the erythrocytes, whereas 65 reacted with human erythrocytes of type A, B, and 0, and 26 with erythrocytes from rabbit, guinea pig, dog, or rat. None of the isolates agglutinated with sheep and goat erythrocytes. The agglutination titres ranged from 0 to 64. Among these isolates, 13 different agglutination patterns could be distinguished. The agglutinating activity was Ca(2+)-dependent and was inhibited by proteases, by temperatures exceeding 50 degrees C and by the addition of D-glucosamine or D-galactosamine. The adherence capacity of the M. catarrhalis isolates to tracheal epithelium correlated with their agglutination titre and could be inhibited by the same treatments. These data provide strong evidence that adherence of M. catarrhalis is mediated by lectins located on the bacterial surface.