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The Journal of Medical Microbiology, Vol 39, Issue 5 388-392, Copyright © 1993 by Society for General Microbiology

JOURNAL ARTICLE

Purification and characterisation of haemagglutinin from Bordetella bronchiseptica

Y. Sakurai, H. Suzuki and E. Terada
Musashino Research Institute for Immunity Co. Ltd, Tokyo, Japan.

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.


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