hly

The N-terminal region is not required for secretion and hemolytic activity, but is involved in phagosomal escape of bacteria in infected cells and is critical for bacterial virulence. This region contains a PEST-like sequence, which does not mediate proteasomal degradation, but controls listeriolysin O production in the cytosol.

A cholesterol-dependent pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Listeriolysin O activates mitogen-activated protein (MAP) kinase activity in host cells, most likely as a result of the permeabilization of the host cell membrane. Also induces a proteasome-independent degradation of UBE2I (the SUMO-conjugating enzyme UBC9) and a proteasome-dependent degradation of some sumoylated proteins. Finally, is necessary and sufficient for spacious Listeria-containing phagosomes (SLAPs) formation, suggesting a role for listeriolysin O in promoting L.monocytogenes replication in vacuoles, leading to persistent infection. Recognized by serum from healthy humans exposed to L.monocytogenes as well from patients who have recovered from listeriosis (PubMed:9284184).

Phosphorylated. Phosphorylation does not appear to be required for ubiquitination or degradation.

Ubiquitinated.

Belongs to the cholesterol-dependent cytolysin family.

• Secreted
• Host membrane
• Multi-pass membrane protein
• Host cell membrane
• Multi-pass membrane protein
• Secreted as soluble protein that then inserts into the host membrane and forms pores formed by transmembrane beta-strands.

hlyA, lisA, lmo0202, hly, Listeriolysin O, LLO, Thiol-activated cytolysin

• swissprot:P13128

Proteins

Immunology & Infectious Disease

58688Da