Final answer:
Listeriolysin O is incorrectly described as a hemolysin that lysates the phagosome in a pH-independent manner. It is a pore-forming toxin, not a phospholipase, and its role differs from that of bacterial phospholipases which degrade the phospholipid bilayer for bacterial escape from phagosomes.
Step-by-step explanation:
The statement that Listeriolysin O is a hemolysin that selectively lyses the phagosome in a pH-independent manner is false. Listeriolysin O, indeed, allows Listeria monocytogenes to escape from the phagosome of a host cell, yet it is not a phospholipase but a pore-forming toxin. It differs from bacterial phospholipases, which degrade the phospholipid bilayer of cell membranes, and from other hemolysins that work synergistically with these phospholipases to lyse cells.
Phospholipases like those produced by B. anthracis and Rickettsia species act upon the phospholipid bilayer of host cells and are implicated in degrading the membrane of the phagosome, allowing escape into the cytoplasm. These enzymes are specific to the type of phospholipids they cleave and are instrumental in bacterial virulence, including their ability to cause cellular lysis.