November 1, 1989Journal of General Virology

Hydrolysis of a Series of Synthetic Peptide Substrates by the Human Rhinovirus 14 3C Proteinase, Cloned and Expressed in Escherichia coli

View Full Paper

Ask AI

Bookmark

Population

Human rhinovirus 14 3C proteinase cloned and expressed in Escherichia coli, and synthetic peptide substrates

Design

Preclinical

Authors

DODavid OrrChildren's Health Ireland at Crumlin ALAnna C. J. LongDuke University JKJohn KayBlue Cross Blue Shield Association

Discussion

Member takes

Implication

May support 3C proteinase as HRV antiviral target; animal data leave open clinical translation.

Structured PICO

Population

Human rhinovirus 14 (HRV-14) 3C proteinase cloned and expressed in Escherichia coli, and synthetic peptide substrates

Intervention

Assaying the enzyme against synthetic peptides corresponding to predicted cleavage sites; introducing a Cys->Ser(146) mutation; testing with known proteinase inhibitors

Outcome

Cleavage of synthetic peptides at specific junctions (Gln-Gly, Gln-Ala, Glu-Gly)surrogate

The HRV-14 3C protein is a cysteine proteinase that specifically cleaves at Gln-Gly junctions, with Cys146 likely acting as the active site nucleophile, representing a potential target for antiviral chemotherapy.

Cite This Study

Orr et al. (1989) studied this question.

synapsesocial.com/papers/6a70dda235aa2c282ce23299 https://doi.org/10.1099/0022-1317-70-11-2931

View Full Paper

Ask AI

Bookmark

Hydrolysis of a Series of Synthetic Peptide Substrates by the Human Rhinovirus 14 3C Proteinase, Cloned and Expressed in Escherichia coli

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Hydrolysis of a Series of Synthetic Peptide Substrates by the Human Rhinovirus 14 3C Proteinase, Cloned and Expressed in Escherichia coli

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider