Membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasite Plasmodium falciparum

The secretory pathway in Plasmodium falciparum has evolved to transport proteins to the host cell membrane and to an endosymbiotic organelle, the apicoplast. The latter can occur via the ER or the ER-Golgi route. Here, we study these three routes using proteins Erythrocyte Membrane Protein-1 (PfEMP1), Acyl Carrier Protein (ACP) and glutathione peroxidase-like thioredoxin peroxidase (PfTPxGl) and inhibitors of vesicular transport. As expected, the G protein dependent vesicular fusion inhibitor AlF4- and microtubule destabilizing drug vinblastine block the trafficking of PfEMP-1, a protein secreted to the host cell membrane. However, while both PfTPxGl and ACP are targeted to the apicoplast, only ACP trafficking remains unaffected by these treatments. This implies that G-protein dependent vesicles do not play a role in classical apicoplast protein targeting. Unlike the soluble protein ACP, we show that PfTPxGl is localized to the outermost membrane of the apicoplast. Thus, the parasite apicoplast acquires proteins via two different pathways: first, the vesicular trafficking pathway appears to handle not only secretory proteins, but an apicoplast membrane protein, PfTPxGl. Second, trafficking of apicoplast luminal proteins appear to be independent of G-protein coupled vesicles.

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Membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasite Plasmodium falciparum

10.7287/peerj.preprints.2813 ◽

2017 ◽

Author(s):

Rahul Chaudhari ◽

Vishakha Dey ◽

Aishwarya Narayan ◽

Shobhona Sharma ◽

Swati Patankar

Keyword(s):

Plasmodium Falciparum ◽

Cell Membrane ◽

Membrane Protein ◽

Host Cell ◽

G Protein ◽

Secretory Pathway ◽

Protein Targeting ◽

Acyl Carrier Protein ◽

Secretory Proteins ◽

Host Cell Membrane

The secretory pathway in Plasmodium falciparum has evolved to transport proteins to the host cell membrane and to an endosymbiotic organelle, the apicoplast. The latter can occur via the ER or the ER-Golgi route. Here, we study these three routes using proteins Erythrocyte Membrane Protein-1 (PfEMP1), Acyl Carrier Protein (ACP) and glutathione peroxidase-like thioredoxin peroxidase (PfTPxGl) and inhibitors of vesicular transport. As expected, the G protein dependent vesicular fusion inhibitor AlF4- and microtubule destabilizing drug vinblastine block the trafficking of PfEMP-1, a protein secreted to the host cell membrane. However, while both PfTPxGl and ACP are targeted to the apicoplast, only ACP trafficking remains unaffected by these treatments. This implies that G-protein dependent vesicles do not play a role in classical apicoplast protein targeting. Unlike the soluble protein ACP, we show that PfTPxGl is localized to the outermost membrane of the apicoplast. Thus, the parasite apicoplast acquires proteins via two different pathways: first, the vesicular trafficking pathway appears to handle not only secretory proteins, but an apicoplast membrane protein, PfTPxGl. Second, trafficking of apicoplast luminal proteins appear to be independent of G-protein coupled vesicles.

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Membrane and luminal proteins reach the apicoplast by different trafficking pathways in the malaria parasitePlasmodium falciparum

PeerJ ◽

10.7717/peerj.3128 ◽

2017 ◽

Vol 5 ◽

pp. e3128 ◽

Cited By ~ 7

Author(s):

Rahul Chaudhari ◽

Vishakha Dey ◽

Aishwarya Narayan ◽

Shobhona Sharma ◽

Swati Patankar

Keyword(s):

Cell Membrane ◽

Membrane Protein ◽

Host Cell ◽

G Protein ◽

Secretory Pathway ◽

Protein Targeting ◽

Acyl Carrier Protein ◽

Secretory Proteins ◽

Host Cell Membrane ◽

Endosymbiotic Organelle

The secretory pathway inPlasmodium falciparumhas evolved to transport proteins to the host cell membrane and to an endosymbiotic organelle, the apicoplast. The latter can occur via the ER or the ER-Golgi route. Here, we study these three routes using proteins Erythrocyte Membrane Protein-1 (PfEMP1), Acyl Carrier Protein (ACP) and glutathione peroxidase-like thioredoxin peroxidase (PfTPxGl) and inhibitors of vesicular transport. As expected, the G protein-dependent vesicular fusion inhibitor AlF4−and microtubule destabilizing drug vinblastine block the trafficking of PfEMP-1, a protein secreted to the host cell membrane. However, while both PfTPxGland ACP are targeted to the apicoplast, only ACP trafficking remains unaffected by these treatments. This implies that G protein-dependent vesicles do not play a role in classical apicoplast protein targeting. Unlike the soluble protein ACP, we show that PfTPxGlis localized to the outermost membrane of the apicoplast. Thus, the parasite apicoplast acquires proteins via two different pathways: first, the vesicular trafficking pathway appears to handle not only secretory proteins, but an apicoplast membrane protein, PfTPxGl; second, trafficking of apicoplast luminal proteins appear to be independent of G protein-coupled vesicles.

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The ring-infected erythrocyte surface antigen protein of Plasmodium falciparum is phosphorylated upon association with the host cell membrane

Molecular and Biochemical Parasitology ◽

10.1016/0166-6851(90)90206-2 ◽

1990 ◽

Vol 38 (1) ◽

pp. 69-75 ◽

Cited By ~ 36

Author(s):

Micheal Foley ◽

Leecia J. Murray ◽

Robin F. Anders

Keyword(s):

Plasmodium Falciparum ◽

Cell Membrane ◽

Host Cell ◽

Surface Antigen ◽

Infected Erythrocyte ◽

Host Cell Membrane ◽

Erythrocyte Surface ◽

Antigen Protein

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Origins of the parasitophorous vacuole membrane of the malaria parasite, Plasmodium falciparum, in human red blood cells

Journal of Cell Science ◽

10.1242/jcs.102.3.527 ◽

1992 ◽

Vol 102 (3) ◽

pp. 527-532 ◽

Cited By ~ 3

Author(s):

A.R. Dluzewski ◽

G.H. Mitchell ◽

P.R. Fryer ◽

S. Griffiths ◽

R.J. Wilson ◽

...

Keyword(s):

Plasmodium Falciparum ◽

Cell Membrane ◽

Host Cell ◽

Malaria Parasite ◽

Parasitophorous Vacuole ◽

Parasitophorous Vacuole Membrane ◽

Host Cell Membrane ◽

Vacuole Membrane ◽

Parasite Plasmodium ◽

Parasite Plasmodium Falciparum

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.

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A host cell membrane protein, golgin-97, is essential for poxvirus morphogenesis

Virology ◽

10.1016/j.virol.2007.01.003 ◽

2007 ◽

Vol 362 (2) ◽

pp. 421-427 ◽

Cited By ~ 8

Author(s):

Dina Alzhanova ◽

Dennis E. Hruby

Keyword(s):

Cell Membrane ◽

Membrane Protein ◽

Host Cell ◽

Host Cell Membrane ◽

Cell Membrane Protein

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Structural Characterization of Ectodomain G Protein of Respiratory Syncytial Virus and Its Interaction with Heparan Sulfate: Multi-Spectroscopic and In Silico Studies Elucidating Host-Pathogen Interactions

Molecules ◽

10.3390/molecules26237398 ◽

2021 ◽

Vol 26 (23) ◽

pp. 7398

Author(s):

Abu Hamza ◽

Abdus Samad ◽

Md. Ali Imam ◽

Md. Imam Faizan ◽

Anwar Ahmed ◽

...

Keyword(s):

Respiratory Syncytial Virus ◽

Cell Membrane ◽

Heparan Sulfate ◽

Host Cell ◽

G Protein ◽

Transition Curve ◽

Host Cell Membrane ◽

State Process ◽

Host Pathogen ◽

Syncytial Virus

The global burden of disease caused by a respiratory syncytial virus (RSV) is becoming more widely recognized in young children and adults. Heparan sulfate helps in attaching the virion through G protein with the host cell membrane. In this study, we examined the structural changes of ectodomain G protein (edG) in a wide pH range. The absorbance results revealed that protein maintains its tertiary structure at physiological and highly acidic and alkaline pH. However, visible aggregation of protein was observed in mild acidic pH. The intrinsic fluorescence study shows no significant change in the λmax except at pH 12.0. The ANS fluorescence of edG at pH 2.0 and 3.0 forms an acid-induced molten globule-like state. The denaturation transition curve monitored by fluorescence spectroscopy revealed that urea and GdmCl induced denaturation native (N) ↔ denatured (D) state follows a two-state process. The fluorescence quenching, molecular docking, and 50 ns simulation measurements suggested that heparan sulfate showed excellent binding affinity to edG. Our binding study provides a preliminary insight into the interaction of edG to the host cell membrane via heparan sulfate. This binding can be inhibited using experimental approaches at the molecular level leading to the prevention of effective host–pathogen interaction.

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