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

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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Binding of a novel cell membrane protein to terminal complement complexes

Immunology Letters ◽

10.1016/s0165-2478(97)87277-x ◽

1997 ◽

Vol 56 (1-3) ◽

pp. 110-111

Author(s):

J Tissari

Keyword(s):

Cell Membrane ◽

Membrane Protein ◽

Cell Membrane Protein ◽

Terminal Complement Complexes ◽

Terminal Complement

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Advances in polarized fluorescence depletion measurement of cell membrane protein rotation

10.1117/12.44208 ◽

1991 ◽

Cited By ~ 2

Author(s):

B. George Barisas ◽

N. A. Rahman ◽

Thomas Londo ◽

J. R. Herman ◽

Deborah A. Roess

Keyword(s):

Cell Membrane ◽

Membrane Protein ◽

Polarized Fluorescence ◽

Cell Membrane Protein

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Deoxygenation affects fluorescence photobleaching recovery measurements of red cell membrane protein lateral mobility

Biophysical Journal ◽

10.1016/s0006-3495(94)80760-x ◽

1994 ◽

Vol 66 (1) ◽

pp. 25-30 ◽

Cited By ~ 18

Author(s):

J.D. Corbett ◽

M.R. Cho ◽

D.E. Golan

Keyword(s):

Cell Membrane ◽

Membrane Protein ◽

Red Cell ◽

Lateral Mobility ◽

Red Cell Membrane ◽

Fluorescence Photobleaching Recovery ◽

Photobleaching Recovery ◽

Cell Membrane Protein

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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.2813v1 ◽

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 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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Metainflammation in COVID-19

Endocrine Metabolic & Immune Disorders - Drug Targets ◽

10.2174/1871530322666220104103325 ◽

2022 ◽

Vol 22 ◽

Author(s):

Mojtaba Bakhtiari ◽

Kamyar Asadipooya

Keyword(s):

Cell Membrane ◽

Viral Entry ◽

Virus Entry ◽

Host Cells ◽

Elderly Men ◽

Virus Binding ◽

Angiotensin Converting Enzyme 2 ◽

Dipeptidyl Peptidase 4 ◽

Beneficial Effects ◽

Binding Capability

Abstract: A new coronavirus pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2], has been on the rise. This virus is fatal for broad groups of populations, including elderly, men, and patients with comorbidities among which obesity is a possible risk factor. The pathophysiologic connections between obesity/metainflammation and COVID-19 may be directly related to increasing soluble ACE2 (angiotensin-converting enzyme 2] levels which potentiates the viral entrance into the host cells, or indirectly related to dysregulation of immune system, microvascular injury and hypercoagulability. The SARS-CoV-2 S-glycoprotein interacts mainly with ACE2 or possibly DDP4 receptors to enter into the host cells. The host proteases, especially TMPRSS2 (transmembrane protease serine 2], support the fusion process and virus entry. While membranous ACE2 is considered a port of entry to the cell for SARS-CoV-2, it seems that soluble ACE2 retains its virus binding capability and enhances its entry into the cells. Interestingly, ACE2 on cell membrane may have protective roles by diminishing cytokine storm-related injuries to the organs. Applying medications that can reduce soluble ACE2 levels, antagonizing TMPRSS2 or blocking DDP4 can improve the outcomes of COVID-19. Metformin and statins through immunomodulatory activities, Orlistat by reducing viral replication, and thiazolidinediones by upregulating ACE2 expression have potential beneficial effects against COVID-19. However, the combination of dipeptidyl peptidase-4 (DDP4] inhibitors and spironolactone/eplerenone seems to be more effective by reducing soluble ACE2 level, antagonizing TMPRSS2, maintaining ACE2 on cell membrane and reducing risk of viral entry into the cells.

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