Malaria is a devastating infectious disease and remains a major public health threat. The causative agents, Plasmodium parasites have a complex lifecycle involving two hosts, transitioning from mosquito to human and requiring the invasion and egress of various host cell types including red blood cells (RBCs). Plasmodium perforin-like protein 2 (PLP2) plays a crucial role in RBC membrane perforation, assisting the escape of parasite gametocytes from RBCs. However, the molecular mechanism of PLP2 targeting the RBC membrane and its oligomerization to form functional pores remains elusive. Here, we show that Plasmodium vivax PLP2(PvPLP2) forms a series of assemblies with variable numbers of subunits(arcs or rings from 16 to 20 subunits) on liposomes and resolve the 3.7 Å structure of the PvPLP2 pore. Cryo-electron tomography reveals that PvPLP2 can form pores on the inner leaflet of red blood cells within a near-native membrane environment. Additionally, the pore-forming activity of PvPLP2 is pH-regulated in vitro. At acidic pH levels, such as pH 5.5, PvPLP2 tends to form stable pre-pore oligomers with variable numbers of subunits, which may represent a structurally inactive state. Our study of PLP2 oligomers in various contexts will enhance our comprehension of PLPs in Plasmodium life cycle.