MOPS and coxsackievirus B3 stability

Steven D. Carson; Susan Hafenstein; Hyunwook Lee

doi:10.1016/j.virol.2016.12.002

MOPS and coxsackievirus B3 stability

Steven D. Carson, Susan Hafenstein, Hyunwook Lee

The Hormel Institute

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

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.

Original language	English (US)
Pages (from-to)	183-187
Number of pages	5
Journal	Virology
Volume	501
DOIs	https://doi.org/10.1016/j.virol.2016.12.002
State	Published - Jan 15 2017

Bibliographical note

Publisher Copyright:
© 2016 Elsevier Inc.

Keywords

Coxsackievirus
MOPS
Stability
pH

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10.1016/j.virol.2016.12.002

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title = "MOPS and coxsackievirus B3 stability",

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.",

keywords = "Coxsackievirus, MOPS, Stability, pH",

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doi = "10.1016/j.virol.2016.12.002",

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T1 - MOPS and coxsackievirus B3 stability

AU - Carson, Steven D.

AU - Hafenstein, Susan

AU - Lee, Hyunwook

PY - 2017/1/15

Y1 - 2017/1/15

N2 - 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.

AB - 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.

KW - Coxsackievirus

KW - MOPS

KW - Stability

KW - pH

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MOPS and coxsackievirus B3 stability

Abstract

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Keywords

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