Characterization of two forms of hemagglutinin/protease produced by Vibrio cholerae non-O1 |
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Authors: | Atsuko Naka Koichiro Yamamoto Toshio Miwatani Takeshi Honda |
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Institution: | Research Institute for Microbial Diseases, Osaka University, Japan. |
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Abstract: | Two forms (34 kDa and 32 kDa) of hemagglutinin/protease produced by Vibrio cholerae non-O1 were characterized. The hemagglutinin/protease purified by immunoaffinity column chromatography using a monoclonal antibody was essentially a 34-kDa form. By incubation of the purified 34-kDa form at 37 degrees C, it was processed (autodigested) to the 32-kDa form. The N-terminal 20 amino acid sequences of both the 34- and 32-kDa forms were identical, suggesting that proteolytic processing at the C-terminal region of the 34-kDa hemagglutinin/protease resulted in the 32-kDa form. With this shift, protease activity increased, but hemagglutinating activity decreased, suggesting that the C-terminal region of the hemagglutinin/protease is related to hemagglutinating activity. |
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Keywords: | Vibrio cholerae non-O1 Protease Hemagglutinin Vibrio cholerae O1 |
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