Abstract:We study the hemolytic activity of a hemolysin protein (HpmA) secreted by the gram negative bacterium Proteus mirabilis. HpmA is the A component of a type Vb, or two‐partner, secretion pathway (TPS pathway). To cross the outer membrane, unfolded periplasmic HpmA is recognized, exported, and folded by its membrane bound cognate B component. Once secreted, HpmA displays cytotoxic activity against mammalian cells, including red blood cells. HpmA is comprised of 1577 amino acids and contains at least two functiona… Show more
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