Plasmodium vivax and P. chabaudi: inter-species cross-reacting antigens

Pérez, H.; Guzmán-Bracho, Carmen; Romano, Mirtha; Rosa, Mercedes de la

doi:10.1007/s004360050241

Cited by 3 publications

(2 citation statements)

References 23 publications

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“…The IgG1 monoclonal antibody (mAb) raised against flotillin-2 of human origin was obtained from BD Biosciences (San Diego, CA, USA). The IgM 7C5B71 mAb which identifies the 148-kDa P. vivax (Pv-148) protein was produced previously in our laboratory (Perez et al 1997;Bracho et al 2002).…”

Section: Primary Antibodiesmentioning

confidence: 99%

Caveolins and flotillin-2 are present in the blood stages of Plasmodium vivax

et al. 2006

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Blood stages of Plasmodium vivax induce the development of caveolae and caveola-vesicle complexes (CVC) in the membrane of their host erythrocyte. Caveolae are found in almost all types of cells and are involved in endogenous processes as calcium and cholesterol homeostasis, cell signalling, transporting, ligand internalization and transcytosis of serum components. Major structural components of caveolae are the proteins caveolins and flotillins. The functional role of caveolae in the P. vivax-infected erythrocyte is not properly understood. As these organelles have been shown to contain malaria antigens, it has been suggested that they are involved in the transport and release of specific parasite antigens from the infected erythrocyte and in the uptake of plasma proteins. Using specific antibodies to classical caveolae proteins and an immunolocalization approach, we found caveolin-2, caveolin-3, and flotillin-2 in the vesicle profiles and some CVC of P. vivax-infected erythrocytes. Caveolin-1-3 were not found in uninfected erythrocytes. This is the first report of identification and localization of caveolins in the CVC present in erythrocytes infected with P. vivax, thereby providing evidence of the role of this particular organelle in the protein-trafficking pathway that connect parasite-encoded proteins with the erythrocyte cytoplasm and the cell surface throughout the asexual blood cycle of vivax malaria parasite.

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Section: Primary Antibodiesmentioning

confidence: 99%

Caveolins and flotillin-2 are present in the blood stages of Plasmodium vivax

et al. 2006

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“…(Pv-148), was produced previously in our laboratory by intrasplenic immunisation of BALB/c mice with human erythrocytes infected with P. vivax (Perez et al 1997). It was partially purified from ascitic fluids by precipitation with ammonium sulfate.…”

Section: Methodsmentioning

confidence: 99%

Traffic pathways of Plasmodium vivax antigens during intraerythrocytic parasite development

Guzmán-Bracho

Dunia

Rosa

et al. 2002

Parasitology Research

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We investigated the secretory traffic of a Plasmodium vivax antigen (Pv-148) synthesised by the parasite during the blood cycle, exported into the host cell cytosol and then transported to the surface membrane of the infected erythrocyte. Studies of the ultrastructure of erythrocytes infected with P. vivax showed that intracellular schizogony is accompanied by the generation of parasite-induced membrane profiles in the erythrocyte cytoplasm. These structures are detectable soon after the parasite invades the erythrocyte and develop an elaborate organisation, leading to a tubovesicular membrane (TVM) network, in erythrocytes infected with mature trophozoites. Interestingly, the clefts formed stacked, flattened cisternae resembling a classical Golgi apparatus. The TVM network stained with the fluorescent Golgi marker Bodipy-ceramide. Specific immunolabelling showed that Pv-148 was transferred from the parasite to the erythrocyte surface membrane via the clefts and the TVM network. These findings suggest that the TVM network is part of the secretory pathways involved in parasite protein transport across the Plasmodium-infected erythrocyte and that Pv- 148 may represent a marker that links the parasite with the host cell cytoplasm and, in turn, with the extracellular milieu.

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