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 languageEnglish (US)
Pages (from-to)183-187
Number of pages5
JournalVirology
Volume501
DOIs
StatePublished - Jan 15 2017

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Enterovirus
Viruses
Molecular Computers
Sulfonic Acids
Capsid
Capsid Proteins
morpholinopropane sulfonic acid
Hydrogen

All Science Journal Classification (ASJC) codes

  • Virology

Cite this

Carson, Steven D. ; Hafenstein, Susan ; Lee, Hyunwook. / MOPS and coxsackievirus B3 stability. In: Virology. 2017 ; Vol. 501. pp. 183-187.
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MOPS and coxsackievirus B3 stability. / Carson, Steven D.; Hafenstein, Susan; Lee, Hyunwook.

In: Virology, Vol. 501, 15.01.2017, p. 183-187.

Research output: Contribution to journalArticle

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