Figure 4.
A P O L 3 interacts with calmodulin-like N M 2 A myosin R L C and E L C, and B C L 2-like B c l-x L. G B P 1 interacts with calmodulin-like N M 2 A myosin R L C and E L C, and B C L 2-like M C L-1. Both proteins bind to cardiolipin, facilitating the permeabilization of the parasitophorous vacuole or pathogen membrane. The diagram shows arrows indicating the interactions and synergistic effects between these proteins.
Synergistic APOL3 and GBP1 activities. Both proteins participate in the permeabilization of intracellular bacterial membranes (11). Given their common interaction properties (double arrowheads), they could hypothetically also participate in permeabilization of various pathogen-surrounding phagosomal membranes (73, 74, 75), promoting both inflammation and antigen cross-presentation. Of note, cardiolipin and calmodulin share the same binding sites, including in the myosin heavy chain (69).