Label-Free Detection of Protein-Protein Interactions on Biochips

2005 ◽  
Vol 44 (34) ◽  
pp. 5480-5483 ◽  
Author(s):  
Woon-Seok Yeo ◽  
Dal-Hee Min ◽  
Robert W. Hsieh ◽  
Geoffrey L. Greene ◽  
Milan Mrksich
Keyword(s):  
Protein Interactions ◽  
Label Free ◽  
Protein Protein Interactions ◽  
Label Free Detection

scholarly journals Label-Free Detection of Single Protein Molecules and Protein−Protein Interactions Using Synthetic Nanopores

2008 ◽  
Vol 80 (12) ◽  
pp. 4651-4658 ◽  
Author(s):  
Anpan Han ◽  
Marc Creus ◽  
Gregor Schürmann ◽  
Vincent Linder ◽  
Thomas R. Ward ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Label Free ◽  
Protein Protein Interactions ◽  
Label Free Detection ◽  
Protein Molecules ◽  
Single Protein

scholarly journals Vertical Scanning Interferometry for Label-Free Detection of Peptide-Antibody Interactions

2019 ◽  
Vol 8 (2) ◽  
pp. 7
Author(s):  
Andrea Palermo ◽  
Richard Thelen ◽  
Laura Weber ◽  
Tobias Foertsch ◽  
Simone Rentschler ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Antibody Concentration ◽  
Label Free ◽  
Protein Protein Interactions ◽  
Peptide Arrays ◽  
Serum Dilution ◽  
Aspect Ratios ◽  
Peptide Antibody ◽  
Label Free Detection ◽  
Vertical Scanning Interferometry

Peptide microarrays are a fast-developing field enabling the mapping of linear epitopes in the immune response to vaccinations or diseases and high throughput studying of protein-protein interactions. In this respect, a rapid label-free measurement of protein layer topographies in the array format is of great interest but is also a great challenge due to the extremely low aspect ratios of the peptide spots. We have demonstrated the potential of vertical scanning interferometry (VSI) for a detailed morphological analysis of peptide arrays and binding antibodies. The VSI technique is shown to scan an array area of 5.1 square millimeters within 3–4 min at a resolution of 1.4 μm lateral and 0.1 nm vertical in the full automation mode. Topographies obtained by VSI do match the one obtained by AFM measurements, demonstrating the accuracy of the technique. A detailed topology of peptide-antibody layers on single spots was measured. Two different measurement regions are distinguished according to the antibody concentration. In the case of weakly diluted serum, the thickness of the antibody layer is independent of the serum dilution and corresponds to the physical thickness of the accumulated antibody layer. In strongly diluted serum, the thickness measured via VSI is linearly proportional to the serum dilution.

scholarly journals Label-free detection of protein-protein interactions using a calmodulin-modified nanowire transistor

2009 ◽  
Vol 107 (3) ◽  
pp. 1047-1052 ◽  
Author(s):  
T.-W. Lin ◽  
P.-J. Hsieh ◽  
C.-L. Lin ◽  
Y.-Y. Fang ◽  
J.-X. Yang ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Label Free ◽  
Protein Protein Interactions ◽  
Nanowire Transistor ◽  
Label Free Detection

Label-Free Detection of Protein-Protein Interactions on Biochips

2005 ◽  
Vol 117 (34) ◽  
pp. 5616-5619 ◽  
Author(s):  
Woon-Seok Yeo ◽  
Dal-Hee Min ◽  
Robert W. Hsieh ◽  
Geoffrey L. Greene ◽  
Milan Mrksich
Keyword(s):  
Protein Interactions ◽  
Label Free ◽  
Protein Protein Interactions ◽  
Label Free Detection

scholarly journals Analysis of Zika virus capsid-Aedes aegypti mosquito interactome reveals pro-viral host factors critical for establishing infection

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Rommel J. Gestuveo ◽  
Jamie Royle ◽  
Claire L. Donald ◽  
Douglas J. Lamont ◽  
Edward C. Hutchinson ◽  
...  
Keyword(s):  
Aedes Aegypti ◽  
Protein Interactions ◽  
Zika Virus ◽  
Label Free ◽  
Protein Protein Interactions ◽  
Zikv Infection ◽  
Ubiquitin Protein Ligase ◽  
Mosquito Cells ◽  
Endoplasmic Reticulum Protein ◽  
Arboviral Diseases

AbstractThe escalating global prevalence of arboviral diseases emphasizes the need to improve our understanding of their biology. Research in this area has been hindered by the lack of molecular tools for studying virus-mosquito interactions. Here, we develop an Aedes aegypti cell line which stably expresses Zika virus (ZIKV) capsid proteins in order to study virus-vector protein-protein interactions through quantitative label-free proteomics. We identify 157 interactors and show that eight have potentially pro-viral activity during ZIKV infection in mosquito cells. Notably, silencing of transitional endoplasmic reticulum protein TER94 prevents ZIKV capsid degradation and significantly reduces viral replication. Similar results are observed if the TER94 ortholog (VCP) functioning is blocked with inhibitors in human cells. In addition, we show that an E3 ubiquitin-protein ligase, UBR5, mediates the interaction between TER94 and ZIKV capsid. Our study demonstrates a pro-viral function for TER94/VCP during ZIKV infection that is conserved between human and mosquito cells.

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