Purification and characterisation of haemagglutinin from Bordetella bronchiseptica.
A surface protein of Bordetella bronchiseptica was purified in one step by affinity chromatography with bovine submaxillary mucin coupled to agarose. The purified protein, with a mol. wt of 200 kDa and an iso-electric point of pI 6.5, showed haemagglutinating activity for bovine erythrocytes. This haemagglutinin (HA) inhibited the adherence of B. bronchiseptica to a rat lung cell line (L2) and was able to bind to N-acetylneuraminic acid. These findings suggest that the HA of B. bronchiseptica is an adhesin.
Sakurai
Y
Y
Musashino Research Institute for Immunity Co. Ltd, Tokyo, Japan.
Suzuki
H
H
Terada
E
E
D000818:Animals; D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D001667:Binding, Competitive; D016950:Bordetella bronchiseptica / Q000472:pathogenicity*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006168:Guinea Pigs; D006386:Hemagglutination Tests; D006388:Hemagglutinins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; D006388:Hemagglutinins