Experiments and simulation on ZIKV NS2B-NS3 protease reveal its complex folding.

Area of Science:

• Virology
• Structural Biology
• Biochemistry

Background:

• Zika virus is found in various body fluids with differing pH levels.
• Understanding viral protein function under various conditions is crucial.

Purpose of the Study:

• To investigate the stability and activity of the Zika virus NS2B-NS3 protease.
• To determine the impact of varying pH and denaturing environments on protease function.

Main Methods:

• Assessed NS2B-NS3 protease stability and activity across a pH range of 4.8-8.7.
• Examined structural changes in the presence of alcohol using spectroscopic methods.

Main Results:

• The NS2B-NS3 protease demonstrated stability and maintained hydrolytic activity within a broad pH range (4.8-8.7).
• Environmental factors, particularly alcohol, induced significant structural alterations, increasing beta-strand and helix content.

Conclusions:

• The Zika virus NS2B-NS3 protease is functionally active in diverse pH environments found in body fluids.
• Protease activity and structure are sensitive to denaturing agents, impacting polyprotein hydrolysis.
• Findings contribute to understanding flaviviral protease folding-function relationships.