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. 1990 May;58(5):1195–1200. doi: 10.1128/iai.58.5.1195-1200.1990

Synthesis and secretion of Bordetella pertussis adenylate cyclase as a 200-kilodalton protein.

J Bellalou 1, D Ladant 1, H Sakamoto 1
PMCID: PMC258609  PMID: 2323814

Abstract

Bordetella pertussis, the etiological agent of whooping cough, synthesizes a calmodulin-sensitive adenylate cyclase that is suspected to play a major role in the virulence of this bacterium. We show that adenylate cyclase synthesized as a 200-kilodalton protein is the product of the cyaA gene and that various virulent Bordetella species secrete this high-molecular-weight polypeptide without apparent proteolytic processing. When submitted to trypsin digestion, the 200-kilodalton protein was converted to a stable 45- to 50-kilodalton species. This corresponds to the size of the enzyme previously purified from a culture supernatant. The molecular heterogeneity reported for the various identified forms of adenylate cyclase could therefore result in part from proteolytic degradation or molecular aggregation of the major 200-kilodalton form of the enzyme.

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Selected References

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