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Last update 23 Jan 2025

HRV 3C protease

Last update 23 Jan 2025

Basic Info

Synonyms

Genome polyprotein, Protein 3B, Viral protein genome-linked

Introduction-

Drugs associated with HRV 3C protease

Rhinovirus inhibitors (eXegenics)

Target

HRV 3C protease

Mechanism

HRV 3C protease inhibitors

Active Org.-

Originator Org.

eXegenics, Inc.

Active Indication-

Inactive Indication

Rhinovirus infection

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Rupintrivir

Target

HRV 3C protease

Mechanism

HRV 3C protease inhibitors

Active Org.-

Originator Org.

Pfizer Inc.

Active Indication-

Inactive Indication

Common Cold [+1]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Imocitrelvir

Target

HRV 3C protease

Mechanism

HRV 3C protease inhibitors

Active Org.-

Originator Org.

Agouron Pharmaceuticals LLC

Active Indication-

Inactive Indication

Rhinovirus infection

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with HRV 3C protease

100 Translational Medicine associated with HRV 3C protease

0 Patents (Medical) associated with HRV 3C protease

Literatures (Medical) associated with HRV 3C protease

01 Dec 2024·Biotechnology Letters

Plant production of recombinant antigens containing the receptor binding domain (RBD) of two SARS-CoV-2 variants

Article

Author: Salzano, Anna Maria ; Donini, Marcello ; Frigerio, Rachele ; Fagiani, Flavia ; Marusic, Carla ; Scaloni, Andrea

OBJECTIVESThe aim of this work was to rapidly produce in plats two recombinant antigens (RBDw-Fc and RBDo-Fc) containing the receptor binding domain (RBD) of the spike (S) protein from SARS-CoV-2 variants Wuhan and Omicron as fusion proteins to the Fc portion of a murine IgG2a antibody constant region (Fc).RESULTSThe two recombinant antigens were expressed in Nicotiana benthamiana plants, engineered to avoid the addition of N-linked plant-typical sugars, through vacuum agroinfiltration and showed comparable purification yields (about 35 mg/kg leaf fresh weight).CONCLUSIONSTheir Western blotting and Coomassie staining evidenced the occurrence of major in planta proteolysis in the region between the RBD and Fc, which was particularly evident in RBDw-Fc, the only antigen bearing the HRV 3C cysteine protease recognition site. The two RBD N-linked glycosylation sites showed very homogeneous profiles free from plant-typical sugars, with the most abundant glycoform represented by the complex sugar GlcNAc₄Man₃. Both antigens were specifically recognised in Western Blot analysis by the anti-SARS-CoV-2 human neutralizing monoclonal antibody J08-MUT and RBDw-Fc was successfully used in competitive ELISA experiments for binding to the angiotensin-converting enzyme 2 receptor to verify the neutralizing capacity of the serum from vaccinated patients. Both SARS-Cov-2 antigens fused to a murine Fc region were rapidly and functionally produced in plants with potential applications in diagnostics.

01 Dec 2024·Protein Expression and Purification

Single-step purification and characterization of Pseudomonas aeruginosa azurin

Article

Author: Vlček, Antonín ; Sýkora, Jan ; Horváth, Matej ; Riegerová, Petra ; Šebesta, Filip ; Šulc, Miroslav

Azurin is a small periplasmic blue copper protein found in bacterial strains such as Pseudomonas and Alcaligenes where it facilitates denitrification. Azurin is extensively studied for its ability to mediate electron-transfer processes, but it has also sparked interest of the pharmaceutical community as a potential antimicrobial or anticancer agent. Here we offer a novel approach for expression and single-step purification of azurin in Escherichia coli with high yields and optimal metalation. A fusion tag strategy using an N-terminal GST tag was employed to obtain pure protein without requiring any additional purification steps. After the on-column cleavage by HRV 3C Protease, azurin is collected and additionally incubated with copper sulphate to ensure sufficient metalation. UV-VIS absorption, mass spectroscopy, and circular dichroism analysis all validated the effective production of azurin, appropriate protein folding and the development of an active site with an associated cofactor. MD simulations verified that incorporation of the N-terminal GPLGS segment does not affect azurin structure. In addition, the biological activity of azurin was tested in HeLa cells.

08 May 2024·Journal of Agricultural and Food Chemistry

Development of a Universal One-Step Purification and Activation Method to Engineer Protein-Glutaminase through Rational Design

Article

Author: Cui, Xin ; Du, Chao ; Rahim, Kashif ; Zhang, Guimin ; Shen, Xingyu ; Li, Xiaodi

Cytotoxic enzymes often exist as zymogens containing prodomains to keep them in an inactive state. Protein-glutaminase (PG), which can enhance various functional characteristics of food proteins, is an enzyme containing pro-PG and mature-PG (mPG). However, poor activity and stability limit its application while tedious purification and activation steps limit its high-throughput engineering. Here, based on structural analysis, we replaced the linker sequence between pro-PG and mPG with the HRV3C protease recognition sequence and then coexpressed it with HRV3C protease in Escherichia coli to develop an efficient one-step purification and activation method for PG. We then used this method to obtain several mutants designed by a combination of computer-aided approach and beneficial point mutations. The specific activity (131.6 U/mg) of the best variant D1 was 4.14-fold that of the wild type, and t_1/2 and T₅₀¹⁰ increased by 13 min and 7 °C, respectively. D1 could effectively improve the solubility and emulsification of wheat proteins, more than twice the effect of the wild type. We also discussed the mechanism underlying the improved properties of D1. In summary, we not only provide a universal one-step purification and activation method to facilitate zymogen engineering but also obtain an excellent PG mutant.

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HRV 3C protease

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