GNLY is transferred to the phagosome

Stable Identifier
Reaction [omitted]
Homo sapiens
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The antimicrobial protein granulysin (GNLY) is secreted from activated human cytotoxic T lymphocytes (CTL) and natural killer (NK) cells (Pena SV et al. 1997; Stenger S et al. 1998; Hanson DA et al. 1999; Ogawa K et al. 2003). The cationic GNLY binds to negatively charged surfaces found in bacteria causing defects in membranes of extracellular and intracellular pathogs (Stenger S et al. 1998; Ernst WA et al. 2000; Barman H et al. 2006). While showing strong antimicrobial activity, GNLY does not permeabilize cell membranes with eukaryotic lipid composition (Barman H et al. 2006). GNLY bound to lipid rafts or phospholipid on eukaryotic cell membranes can be internalized by lipid rafts and delivered to the early sorting endosomes which afterwards fuse with bacteria-containing phagosomes, where the GNLY-mediated lysis of bacteria is induced (Walch M et al. 2005, 2007). GNLY may require perforin as a cofactor to enter the host cells (Stenger S et al. 1998) However, it was also suggested that perforin promotes GNLY-mediated bacteriolysis not by the formation of stable pores that allow passive diffusion of GNLS but rather by an increase in endosome-phagosomes fusion triggered by an intracellular Ca(2+) rise (Walch M et al. 2007).
Literature References
PubMed ID Title Journal Year
15778384 Uptake of granulysin via lipid rafts leads to lysis of intracellular Listeria innocua

Barman, H, Ziegler, U, Groscurth, P, Eppler, E, Walch, M, Dumrese, C

J. Immunol. 2005
Orthologous Events
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