Twelve diverse strains of of clinical origin all produced a calcium-dependent haemolysin, unlike most other spp. In most strains the haemolysin was secreted into the medium during early exponential growth and lysed not only of a variety of erythrocyte types from several animals including man, but also human neutrophils and human embryo lung fibroblasts. The haemolysin was a protein of 107 kDa, the same size as H1yA, and it reacted with antiserum to H1yA. Because of its similarity in size, antigenicity and range of action to the H1yA virulence factor of H1yA is believed to be an important virulence factor for this organism. It was degradable by an EDTA-sensitive protease—probably the IgA protease—to inactive fragments. The interaction of H1yA and IgA protease and the origin of H1yA, which has now been found in many diverse bacteria, are discussed.


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