scholarly journals Characterization of the SARS‐CoV‐2 E Protein: Sequence, Structure, Viroporin and Inhibitors

2021 ◽  
Author(s):  
Yipeng Cao ◽  
Rui Yang ◽  
Imshik Lee ◽  
Wenwen Zhang ◽  
Jiana Sun ◽  
...  
Keyword(s):  
Protein Sequence ◽  
Sequence Structure ◽  
E Protein

scholarly journals Biophysical characterization of the SARS-CoV-2 E protein

2021 ◽  
Author(s):  
Aujan Mehregan ◽  
Sergio Perez-Conesa ◽  
Yuxuan Zhuang ◽  
Ahmad Elbahnsi ◽  
Diletta Pasini ◽  
...  
Keyword(s):  
Recombinant Expression ◽  
Structural Data ◽  
Md Simulations ◽  
Full Length ◽  
Coarse Grained ◽  
Biophysical Characterization ◽  
Viral Budding ◽  
Nmr Structures ◽  
E Protein

SARS-CoV-2 is the virus responsible for the COVID-19 pandemic which continues to wreak havoc across the world, over a year and a half after its effects were first reported in the general media. Current fundamental research efforts largely focus on the SARS-CoV-2 Spike protein. Since successful antiviral therapies are likely to target multiple viral components, there is considerable interest in understanding the biophysical role of its other proteins, in particular structural membrane proteins. Here, we have focused our efforts on the characterization of the full-length E protein from SARS-CoV-2, combining experimental and computational approaches. Recombinant expression of the full-length E protein from SARS-CoV-2 reveals that this membrane protein is capable of independent multimerization, possibly as a tetrameric or smaller species. Fluorescence microscopy shows that the protein localizes intracellularly, and coarse-grained MD simulations indicate it causes bending of the surrounding lipid bilayer, corroborating a potential role for the E protein in viral budding. Although we did not find robust electrophysiological evidence of ion-channel activity, cells transfected with the E protein exhibited reduced intracellular Ca2+, which may further promote viral replication. However, our atomistic MD simulations revealed that previous NMR structures are relatively unstable, and result in models incapable of ion conduction. Our study highlights the importance of using high-resolution structural data obtained from a full-length protein to gain detailed molecular insights, and eventually permitting virtual drug screening.

Sequence-structure characterization of recombinant polypeptides derived from silk fibroin heavy chain

2020 ◽  
Vol 111 ◽  
pp. 110831
Author(s):  
Jingjing Xu ◽  
Yining Wang ◽  
Mengyao Ding ◽  
Guangzhou Song ◽  
Mingyang Wu ◽  
...  
Keyword(s):  
Silk Fibroin ◽  
Heavy Chain ◽  
Structure Characterization ◽  
Sequence Structure ◽  
Recombinant Polypeptides
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