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April 20, 2005Acta Crystallographica Section D Biological CrystallographyOpen Access

Crystallization of foot-and-mouth disease virus 3C protease: surface mutagenesis and a novel crystal-optimization strategy

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Key result

Targeted mutagenesis of surface amino acids combined with iterative screening yielded a foot-and-mouth disease virus 3C protease construct amenable to crystallization with 1.9 A diffraction.

Population

Foot-and-mouth disease virus (FMDV) 3C protease (3C(pro))

Comparison

Targeted mutagenesis of surface amino acids… vs Purified wild-type protein

Design

Preclinical

Authors

JBJames R. BirtleySCStephen Curry

Discussion

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Overview

May enable FMDV 3C structural biology for antivirals; leaves open translation in disease models.

Structured PICO

P
Population
Foot-and-mouth disease virus (FMDV) 3C protease (3C(pro))
I
Intervention
Targeted mutagenesis of surface amino acids (substitution of two Cys residues) combined with trimming of N- and C-termini, and 'iterative screening' using commercial crystal screening solutions as additives
C
Comparator
Purified wild-type protein
O
Outcome
Crystallization and high-resolution diffraction

The study provides a novel crystal-optimization strategy and construct for FMDV 3C protease, enabling structural studies for antiviral drug targeting.

Cite This Study

Birtley et al. (2005) studied Foot-and-mouth disease virus (FMDV). Targeted mutagenesis and iterative screening vs. Wild-type protein was evaluated on Crystallization and high-resolution diffraction. Targeted mutagenesis of surface amino acids combined with iterative screening yielded a foot-and-mouth disease virus 3C protease construct amenable to crystallization with 1.9 A diffraction.

synapsesocial.com/papers/6a9ea3dc73165503c06a7ca4https://doi.org/10.1107/s0907444905007924
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