Ace2 Tmprss2
Ace2 Tmprss2 - Related Videos
05:30
Assessing Functional SARS-CoV-2 Neutralizing Antibodies
0 Views •
2026
Source:Kelly Da Costa1, Diego Cantoni1,2, Martin Mayora-Neto1, Tobia Fantoni1,3, Nigel Temperton11Viral Pseudotype Unit, Medway School of Pharmacy, University of Kent.2MRC-University of Glasgow Centre for Virus Research, University of Glasgow.3Department of Neurosciences, Biomedicine and Movement Sciences, University of Verona.This video showcases a neutralization assay measuring serum efficacy in neutralizing SARS-CoV-2 viruses. It involves pseudotyped viruses, serum dilution, and...
02:46
Visualizing Dose-Dependent Spike Protein Uptake with Quantum Dot Conjugates
0 Views •
2026
Source: Tran, B. N., et. al. High-throughput Confocal Imaging of Quantum Dot-Conjugated SARS-CoV-2 Spike Trimers to Track Binding and Endocytosis in HEK293T Cells. J. Vis. Exp. (2022)This video demonstrates the use of quantum dot–conjugated spike protein (QD-Spike) to visualize dose-dependent viral entry in ACE2-GFP–expressing cells. Confocal imaging captures the internalization of QD-Spike via receptor-mediated endocytosis, modeling early coronavirus entry.
03:11
Bioreporter Assay: A Sensitive Technique using a Bioluminescent Reporter System to Detect SARS-CoV-2 Antibodies
0 Views •
2025
In this video, we show the HiBit-RBD bioreporter system-based assay for detecting SARS-CoV-2 neutralizing antibodies. This system targets the viral RBD domain by using a bioluminescent reporter system containing HiBiT fused to the RBD domain.
FAQs
ACE2 provides the cell-surface contact point, while TMPRSS2 acts on the viral spike after receptor engagement. Cleavage of the spike initiates structural rearrangements that make fusion between the viral envelope and host-cell membrane possible. Thus, receptor recognition and proteolytic activation represent successive biochemical contributions to the same entry route.
Coordinated activity can help explain why some cell populations are more relevant to infection than others. Differences in the presence or functional activity of these two proteins may influence whether the viral entry pathway can proceed, making the pair useful for investigating viral tropism and host susceptibility. This connection is particularly relevant in respiratory epithelial cells.
ACE2 and TMPRSS2 are not interchangeable components. ACE2 supplies receptor function at the cell surface, whereas TMPRSS2 supplies proteolytic activity directed at viral spike protein. Studying them separately and together helps clarify whether a change affects recognition, spike activation, or the fusion step that follows. This division of labor is central to biochemical interpretation.
Respiratory epithelial cells provide an important biological context for examining this pathway because their coordinated ACE2 and TMPRSS2 activity is especially relevant to viral entry. Experiments using this context can connect molecular events, such as spike cleavage and membrane fusion, with broader questions about viral tropism and host susceptibility rather than treating entry as an isolated reaction.
Biochemical analyses can focus on molecular interaction and spike-cleavage steps, while cell-based analyses examine how those events relate to entry in a cellular setting. Considering both levels helps researchers connect protein function with membrane fusion and assess whether observations remain relevant to respiratory epithelial cells. Together, they provide complementary evidence about the entry pathway.
Entry inhibitors are evaluated by asking whether they interfere with the ACE2 and TMPRSS2 pathway or the associated spike-driven fusion process. Biochemical and cell-based analyses can therefore provide evidence about how effectively a strategy limits viral entry-related events. This makes the pathway useful for comparing approaches intended to reduce viral transmission or disease.