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Reviews of "Protein arginylation is regulated during SARS-CoV-2 infection"

Reviewers: Fangliang Zhang (University of Miami) | 📒📒📒◻️◻️  • Aaron Smith (University of Maryland) | 📒📒📒◻️◻️ • Hyunjoo Cha-Molstad (Korea Research Institute of Bioscience and Biotechnology)  |📙📙 ◻️◻️◻️

Published onJan 26, 2022
Reviews of "Protein arginylation is regulated during SARS-CoV-2 infection"
key-enterThis Pub is a Review of
Protein arginylation is regulated during SARS-CoV-2 infection

ABSTRACTIn 2019, the world witnessed the onset of an unprecedented pandemic. In September 2021, the infection by SARS-CoV-2 had already been responsible for the death of more than 4 million people worldwide. Recently, we and other groups discovered that SARS-CoV-2 infection induces ER-stress and activation of unfolded protein response (UPR) pathway. The degradation of misfolded/unfolded proteins is an essential element of proteostasis and occurs mainly in lysosomes or proteasomes. The N-terminal arginylation of proteins is characterized as an inducer of ubiquitination and proteasomal degradation by the N-end rule pathway. Here we present, for the first time, data on the role of arginylation during SARS-CoV-2 infection. We studied the modulation of protein arginylation in Vero CCL-81 and Calu-3 cells infected after 2h, 6h, 12h, 24h, and 48h. A reanalysis of in vivo and in vitro public omics data combined with immunoblotting was performed to measure the levels of ATE1 and arginylated proteins. This regulation is seen specifically during infections by coronaviruses. We demonstrate that during SARS-CoV-2 infection there is an increase in the expression of the ATE1 enzyme associated with regulated levels of specific arginylated proteins. On the other hand, infected macrophages showed no ATE1 regulation. An important finding revealed that modulation of the N-end rule pathway differs between different types of infected cells. We also confirmed the potential of tannic acid to reduce viral load, and furthermore, to modulate ATE1 levels during infection. In addition, the arginylation inhibitor merbromin (MER) is also capable of both reducing viral load and reducing ATE1 levels. Taken together, these data show the importance of arginylation during the progression of SARS-CoV-2 infection and open the door for future studies that may unravel the role of ATE1 and its inhibitors in pathogen infection.

To read the original manuscript, click the link above.

Summary of Reviews: This preprint looks at how SARS-CoV-2 infection modulates arginylation, a modification that tags proteins for degradation, and finds a specific arginylation signature in some cell types. The reviewers found the claims potentially informative.

Reviewer 1 (Fangliang Zhang) | 📒📒📒 ◻️◻️

Reviewer 2 (Aaron Smith) | 📒📒📒 ◻️◻️

RR:C19 Strength of Evidence Scale Key

📕 ◻️◻️◻️◻️ = Misleading

📙📙 ◻️◻️◻️ = Not Informative

📒📒📒 ◻️◻️ = Potentially Informative

📗📗📗📗◻️ = Reliable

📘📘📘📘📘 = Strong

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