New Insights into the Functionality of a Virion-Anchored Host Cell Membrane Protein: CD28 Versus HIV Type 1

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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In situ labelling chemistry of respiratory syncytial viruses by employing the biotinylated host-cell membrane protein for tracking the early stage of virus entry

Chemical Communications ◽

10.1039/c4cc06264g ◽

2014 ◽

Vol 50 (99) ◽

pp. 15776-15779 ◽

Cited By ~ 14

Author(s):

Lin Ling Zheng ◽

Xiao Xi Yang ◽

Yue Liu ◽

Xiao Yan Wan ◽

Wen Bi Wu ◽

...

Keyword(s):

Cell Membrane ◽

Membrane Protein ◽

Quantum Dot ◽

Early Stage ◽

Virus Entry ◽

Host Cells ◽

Host Cell Membrane ◽

Respiratory Syncytial Viruses ◽

Cell Membrane Protein

Anin situstrategy for producing quantum dot-labelled respiratory syncytial viruses by incorporating the biotinylated membrane protein of the host cells into mature virions is reported.

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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.2813v2 ◽

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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Human Immunodeficiency Virus Type 1 Nef protein modulates the lipid composition of virions and host cell membrane microdomains

Retrovirology ◽

10.1186/1742-4690-4-70 ◽

2007 ◽

Vol 4 (1) ◽

pp. 70 ◽

Cited By ~ 60

Author(s):

Britta Brügger ◽

Ellen Krautkrämer ◽

Nadine Tibroni ◽

Claudia E Munte ◽

Susanne Rauch ◽

...

Keyword(s):

Human Immunodeficiency Virus ◽

Cell Membrane ◽

Host Cell ◽

Human Immunodeficiency Virus Type ◽

Virus Type ◽

Lipid Composition ◽

Membrane Microdomains ◽

Host Cell Membrane ◽

Immunodeficiency Virus

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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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Candidate screening of host cell membrane proteins involved in SARS-CoV-2 entry

10.1101/2020.09.09.289488 ◽

2020 ◽

Author(s):

Norihiro Kotani ◽

Takanari Nakano

Keyword(s):

Membrane Proteins ◽

Cell Membrane ◽

Host Cell ◽

Viral Entry ◽

Antiviral Agents ◽

Host Cells ◽

Host Cell Membrane ◽

Cell Membrane Proteins ◽

Cell Membrane Protein ◽

Spike Proteins

ABSTRACTCOVID-19 represents a real threat to the global population, and understanding the biological features of the causative virus (SARS-CoV-2) is imperative to aid in mitigating this threat. Analyses of proteins such as primary receptors and co-receptors (co-factors) that are involved in SARS-CoV-2 entry into host cells will provide important clues to help control the virus. Here, we identified host cell membrane protein candidates that were present in proximity to the attachment sites of SARS-CoV-2 spike proteins through the use of proximity labeling and proteomics analysis. The identified proteins represent candidate key factors that may be required for viral entry. Our results indicated that a number of membrane proteins, including DPP4, Cadherin-17, and CD133, were identified to co-localize with cell membrane-bound SARS-CoV-2 spike proteins in Caco-2 cells that were used to expand the SARS-CoV-2 virion. We anticipate that the information regarding these protein candidates will be utilized for the future development of vaccines and antiviral agents against SARS-CoV-2.

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