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J Med Microbiol. 1993 Nov;39(5):388-92.

Purification and characterisation of haemagglutinin from Bordetella bronchiseptica.

Author information

1
Musashino Research Institute for Immunity Co. Ltd, Tokyo, Japan.

Abstract

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.

PMID:
8246255
DOI:
10.1099/00222615-39-5-388
[Indexed for MEDLINE]

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