M. Fitzgerald et al., HEMAGGLUTINATION PROPERTIES OF MORAXELLA (BRANHAMELLA) CATARRHALIS, British journal of biomedical science, 53(4), 1996, pp. 257-262
The ability of 30 isolates of Moraxella (Branhamella) catarrhalis to h
aemagglutinate erythrocytes of five species was examined. Two haemaggl
utination phenotypes of M. catarrhalis were observed: phenotype I isol
ates (n = 10) agglutinated human erythrocytes, while phenotype II isol
ates (n = 7) agglutinated both human and rabbit erythrocytes. No haema
gglutination was observed with chick, sheep or horse erythrocytes. Hae
magglutination by both phenotype I and II isolates was abolished follo
wing treatment of these isolates with pronase and trypsin, while heat
treatment at 70 degrees C markedly reduced the level of haemagglutinat
ion by both sets of isolates. Haemagglutination by phenotype II isolat
es was inhibited by galactose, whereas haemagglutination by phenotype
I isolates was not inhibited by this carbohydrate. Transmission electr
on microscopy (TEM) studies showed that very close cell-surface intera
ctions occurred when both phenotypes of M. catarrhalis adhered to the
human erythrocyte. Fimbrial attachment was not apparent. Haemagglutina
ting isolates of both phenotypes had a trypsin-sensitive outer fibrill
ar coat when examined by TEM.