A late liver stage rodent malaria parasite (left) is surrounded by a parasitophorous vacuole membrane (red) and has a complex apicoplast (green). Parasites lacking genes for apicoplast-targeted phosphatidic acid synthesis are attenuated (right). For furth

2014 ◽  
Vol 91 (4) ◽  
pp. i-i
2013 ◽  
Vol 62 (3) ◽  
pp. 337-340 ◽  
Author(s):  
Miho Usui ◽  
Hirono Masuda-Suganuma ◽  
Shinya Fukumoto ◽  
Jose Ma. M. Angeles ◽  
Noboru Inoue ◽  
...  

1992 ◽  
Vol 102 (3) ◽  
pp. 527-532 ◽  
Author(s):  
A.R. Dluzewski ◽  
G.H. Mitchell ◽  
P.R. Fryer ◽  
S. Griffiths ◽  
R.J. Wilson ◽  
...  

We have attempted to determine whether the parasitophorous vacuole membrane, in which the malaria parasite (merozoite) encapsulates itself when it enters a red blood cell, is derived from the host cell plasma membrane, as the appearance of the invasion process in the electron microscope has been taken to suggest, or from lipid material stored in the merozoite. We have incorporated into the red cell membrane a haptenic phospholipid, phosphatidylethanolamine, containing an NBD (N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)) group, substituted in the acyl chain, and allowed it to translocate into the inner bilayer leaflet. After invasion of these labelled cells by the parasite, Plasmodium falciparum, immuno-gold electron microscopy was used to follow the distribution of the labelled lipid; this was found to be overwhelmingly in favour of the host cell membrane relative to the parasitophorous vacuole. Merozoites of P. knowlesi were allowed to attach irreversibly to red cells without invasion, using the method of pretreatment with cytochalasin. The region of contact between the merozoite and the host cell membrane was in all cases devoid of the labelled phosphatidylethanolamine. These results lead us to infer that the parasitophorous vacuole membrane is derived wholly or partly from lipid preexisting in the merozoite.


2015 ◽  
Vol 11 (3) ◽  
pp. e1004760 ◽  
Author(s):  
Paul-Christian Burda ◽  
Matthias A. Roelli ◽  
Marco Schaffner ◽  
Shahid M. Khan ◽  
Chris J. Janse ◽  
...  

2010 ◽  
Vol 9 (5) ◽  
pp. 784-794 ◽  
Author(s):  
Drew C. MacKellar ◽  
Matthew T. O'Neill ◽  
Ahmed S. I. Aly ◽  
John B. Sacci ◽  
Alan F. Cowman ◽  
...  

ABSTRACT Upregulated in infectious sporozoites gene 4 (UIS4) encodes a parasitophorous vacuole membrane protein expressed in the sporozoite and liver stages of rodent malaria parasites. Parasites that lack UIS4 arrest in early liver-stage development, and vaccination of mice with uis4 − sporozoites confers sterile protection against challenge with infectious sporozoites. Currently, it remains unclear whether an ortholog of UIS4 is carried in the human malaria parasite Plasmodium falciparum, although the gene PF10_0164 has been identified as a candidate ortholog for UIS4 on the basis of synteny and structural similarity of the encoded protein. We show that PF10_0164 is expressed in sporozoites and blood stages of P. falciparum, where it localizes to the parasitophorous vacuole, and is also exported to the host erythrocyte. PF10_0164 is refractory to disruption in asexual blood stages. Functional complementation was tested in Plasmodium yoelii by replacing the endogenous copy of UIS4 with PF10_0164. PF10_0164 localized to the parasitophorous vacuole membrane of liver stages, but transgenic parasites did not complete liver-stage development in mice. We conclude that PF10_0164 is a parasitophorous vacuole protein that is essential in asexual blood stages and that does not complement P. yoelii UIS4, and it is thus likely not a functional ortholog of UIS4.


2013 ◽  
Vol 110 (30) ◽  
pp. E2838-E2847 ◽  
Author(s):  
K. K. Hanson ◽  
A. S. Ressurreicao ◽  
K. Buchholz ◽  
M. Prudencio ◽  
J. D. Herman-Ornelas ◽  
...  

2020 ◽  
Author(s):  
Kayla Sylvester ◽  
Steven P. Maher ◽  
Dora Posfai ◽  
Michael K. Tran ◽  
McKenna C. Crawford ◽  
...  

AbstractThe apicomplexan Plasmodium parasites replicate in the liver before causing malaria. P. vivax can also persist in the liver as dormant hypnozoites and cause relapses upon activation. The host water and solute channel aquaporin-3 (AQP3) has been shown to localize to the parasitophorous vacuole membrane (PVM) of P. vivax hypnozoites and liver schizonts, along with other Plasmodium species and stages. In this study, we use high-resolution microscopy to characterize temporal changes of the tubovesicular network (TVN), a PVM-derived network within the host cytosol, during P. vivax liver-stage infection. We demonstrate an unexpected role for the TVN in hypnozoites and reveal AQP3 associates with TVN-derived vesicles and extended membrane features. We further show AQP3 recruitment to Toxoplasma gondii. Our results highlight dynamic host-parasite interactions that occur in both dormant and replicating liver-stage P. vivax forms and implicate AQP3 function during this time. Together, these findings enhance our understanding of AQP3 in apicomplexan infection.


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