Split-Luciferase Complementation for Analysis of Virus–Host Protein Interactions

2021 ◽  
pp. 55-62
Author(s):  
Yan Liang ◽  
Zhenghe Li
Keyword(s):  
Protein Interactions ◽  
Host Protein ◽  
Split Luciferase Complementation ◽  
Split Luciferase

scholarly journals Split luciferase complementation assay to detect regulated protein-protein interactions in rice protoplasts in a large-scale format

Rice ◽  
2014 ◽  
Vol 7 (1) ◽  
Author(s):  
Yukichi Fujikawa ◽  
Takahiro Nakanishi ◽  
Hiroko Kawakami ◽  
Kanako Yamasaki ◽  
Masa H Sato ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Large Scale ◽  
Protein Protein Interactions ◽  
Complementation Assay ◽  
Split Luciferase Complementation ◽  
Scale Format ◽  
Split Luciferase

LUCIFERASES FOR THE STUDY OF PROTEIN–PROTEIN INTERACTIONS IN LIVE CELLS AND ANIMALS

Nano LIFE ◽  
2010 ◽  
Vol 01 (01n02) ◽  
pp. 79-87 ◽  
Author(s):  
A. K. M. KAFI ◽  
MITSURU HATTORI ◽  
TAKEAKI OZAWA
Keyword(s):  
Transcriptional Regulation ◽  
Protein Interactions ◽  
Protein Modification ◽  
Specific Protein ◽  
Live Cells ◽  
Protein Protein Interactions ◽  
Recent Developments ◽  
Split Luciferase Complementation ◽  
Spatio Temporal ◽  
Split Luciferase

Many imaging technologies based on luminescent proteins have proven useful for detecting protein–protein interactions, tracking cells in mice, and monitoring transcriptional regulation of specific genes. Especially, novel bioluminescent proteins have advanced the study of induced protein interactions and protein modification in live cells and animals. This review focuses on recent developments of bioluminescent probes for quantitative evaluation of specific protein–protein interactions and their spatio-temporal imaging by means of split luciferase complementation techniques. From the comparison between fluorescent and bioluminescent proteins, advantages and drawbacks of the bioluminescence techniques are described.

scholarly journals Application of a split luciferase complementation assay for the detection of viral protein–protein interactions

2011 ◽  
Vol 176 (1-2) ◽  
pp. 108-111 ◽  
Author(s):  
Qiji Deng ◽  
Dan Wang ◽  
Xiaoxiao Xiang ◽  
Xiaofei Gao ◽  
Philip R. Hardwidge ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Viral Protein ◽  
Protein Protein Interactions ◽  
Complementation Assay ◽  
Split Luciferase Complementation ◽  
Split Luciferase

A split luciferase complementation assay for studying in vivo protein–protein interactions in filamentous ascomycetes

2012 ◽  
Vol 58 (3) ◽  
pp. 179-189 ◽  
Author(s):  
Hee-Kyoung Kim ◽  
Eun Ji Cho ◽  
Seong mi Jo ◽  
Bo Reum Sung ◽  
Seunghoon Lee ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Complementation Assay ◽  
Split Luciferase Complementation ◽  
Split Luciferase

scholarly journals Identification of Compounds Targeting Hepatitis B Virus Core Protein Dimerization through a Split Luciferase Complementation Assay

2018 ◽  
Vol 62 (12) ◽  
Author(s):  
Xia-Fei Wei ◽  
Chun-Yang Gan ◽  
Jing Cui ◽  
Ying-Ying Luo ◽  
Xue-Fei Cai ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Protein Interactions ◽  
Core Protein ◽  
Cell Model ◽  
Protein Protein Interactions ◽  
B Virus ◽  
Split Luciferase Complementation ◽  
Split Luciferase

ABSTRACTThe capsid of the hepatitis B virus is an attractive antiviral target for developing therapies against chronic hepatitis B infection. Currently available core protein allosteric modulators (CpAMs) mainly affect one of the two major types of protein-protein interactions involved in the process of capsid assembly, namely, the interaction between the core dimers. Compounds targeting the interaction between two core monomers have not been rigorously screened due to the lack of screening models. We report here a cell-based assay in which the formation of core dimers is indicated by split luciferase complementation (SLC). Making use of this model, 2 compounds, Arbidol (umifenovir) and 20-deoxyingenol, were identified from a library containing 672 compounds as core dimerization regulators. Arbidol and 20-deoxyingenol inhibit the hepatitis B virus (HBV) DNA replicationin vitroby decreasing and increasing the formation of core dimer and capsid, respectively. Our results provided a proof of concept for the cell model to be used to screen new agents targeting the step of core dimer and capsid formation.

scholarly journals Native Structure-Based Peptides as Potential Protein–Protein Interaction Inhibitors of SARS-CoV-2 Spike Protein and Human ACE2 Receptor

Molecules ◽  
2021 ◽  
Vol 26 (8) ◽  
pp. 2157
Author(s):  
Norbert Odolczyk ◽  
Ewa Marzec ◽  
Maria Winiewska-Szajewska ◽  
Jarosław Poznański ◽  
Piotr Zielenkiewicz
Keyword(s):  
Drug Development ◽  
Protein Interactions ◽  
Rna Virus ◽  
Antiviral Drug ◽  
Host Protein ◽  
Host Cells ◽  
Cell Surface Receptor ◽  
Short Peptides ◽  
Virus Protein ◽  
Positive Strand Rna

Severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) is a positive-strand RNA virus that causes severe respiratory syndrome in humans, which is now referred to as coronavirus disease 2019 (COVID-19). Since December 2019, the new pathogen has rapidly spread globally, with over 65 million cases reported to the beginning of December 2020, including over 1.5 million deaths. Unfortunately, currently, there is no specific and effective treatment for COVID-19. As SARS-CoV-2 relies on its spike proteins (S) to bind to a host cell-surface receptor angiotensin-converting enzyme-2(ACE2), and this interaction is proved to be responsible for entering a virus into host cells, it makes an ideal target for antiviral drug development. In this work, we design three very short peptides based on the ACE2 sequence/structure fragments, which may effectively bind to the receptor-binding domain (RBD) of S protein and may, in turn, disrupt the important virus-host protein–protein interactions, blocking early steps of SARS-CoV-2 infection. Two of our peptides bind to virus protein with affinity in nanomolar range, and as very short peptides have great potential for drug development.

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