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Published on: June 16, 2011
MOPS and coxsackievirus B3 stability
Steven D Carson1, Susan Hafenstein2, Hyunwook Lee2
1Department of Pathology and Microbiology University of Nebraska Medical Center, 986495 Nebraska Medical Center, Omaha, NE 68198-6495, USA.
Abstract:
Study of coxsackievirus B3 strain 28 (CVB3/28) stability using MOPS to improve buffering in the experimental medium revealed that MOPS (3-morpholinopropane-1-sulfonic acid) increased CVB3 stability and the effect was concentration dependent. Over the pH range 7.0-7.5, virus stability was affected by both pH and MOPS concentration. Computer-simulated molecular docking showed that MOPS can occupy the hydrophobic pocket in capsid protein VP1 where the sulfonic acid head group can form ionic and hydrogen bonds with Arg95 and Asn211 near the pocket opening. The effects of MOPS and hydrogen ion concentrations on the rate of virus decay were modeled by including corresponding parameters in a recent kinetic model. These results indicate that MOPS can directly associate with CVB3 and stabilize the virus, possibly by altering capsid conformational dynamics.
Insights
MOPS (3-morpholinopropane-1-sulfonic acid) enhances coxsackievirus B3 stability in a concentration-dependent manner. This buffering agent interacts with viral capsid protein VP1, potentially stabilizing the virus by altering its structure.
Area of Science:
- Virology
- Biochemistry
- Physical Chemistry
Background:
- Coxsackievirus B3 (CVB3) is a significant human pathogen.
- Maintaining virus stability in experimental conditions is crucial for research.
- The buffering capacity of experimental media can influence virus stability.
Purpose of the Study:
- To investigate the effect of MOPS (3-morpholinopropane-1-sulfonic acid) on CVB3 stability.
- To elucidate the mechanism by which MOPS influences CVB3 stability.
- To model the impact of MOPS and pH on virus decay kinetics.
Main Methods:
- Experimental assessment of CVB3 stability in the presence of varying MOPS concentrations and pH.
- Computer-simulated molecular docking to predict MOPS-CVB3 interactions.
- Kinetic modeling to analyze virus decay rates.
Main Results:
- MOPS significantly increased CVB3 stability, with effects being concentration-dependent.
- Optimal virus stability was observed within a specific pH range (7.0-7.5) influenced by MOPS concentration.
- Molecular docking revealed MOPS binding to a hydrophobic pocket in capsid protein VP1, forming ionic and hydrogen bonds.
- Kinetic modeling confirmed the influence of MOPS and hydrogen ion concentrations on virus decay.
Conclusions:
- MOPS directly associates with CVB3, enhancing its stability.
- The stabilization mechanism likely involves MOPS binding to VP1 and altering capsid conformational dynamics.
- MOPS is a valuable buffering agent for preserving CVB3 stability in research settings.
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