Open AccessPurification and characterisation of haemagglutinin from Bordetella bronchiseptica
Author(s) -
Yoshinori Sakurai,
Hirofumi Suzuki,
Eiji Terada
Publication year - 1993
Publication title -
journal of medical microbiology/journal of medical microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.91
H-Index - 117
eISSN - 1473-5644
pISSN - 0022-2615
DOI - 10.1099/00222615-39-5-388
Subject(s) - bordetella bronchiseptica , bacterial adhesin , bordetella , microbiology and biotechnology , mucin , affinity chromatography , agarose , biology , chemistry , biochemistry , bacteria , enzyme , escherichia coli , gene , genetics , bordetella pertussis
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.