Albumin enhances the rate at which coxsackievirus B3 strain 28 converts to A-particles

Steven D. Carson, Andrew J. Cole

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

Three strains of coxsackievirus B3 (CVB3) differ by single mutations in capsid protein VP1 or VP3 and also differ in stability at 37°C in tissue culture medium. Among these strains, the CVB3/28 parent strain has been found to be uniquely sensitive to a component in fetal bovine serum (FBS) identified as serum albumin. In cell culture medium, serum increased the rate of CVB3/28 conversion to noninfectious particles at least 2-fold. The effect showed a saturable dose response. Rates of conversion to noninfectious virus with high concentrations of soluble coxsackievirus and adenovirus receptor (sCAR) were similar with and without FBS, but FBS amplified the catalytic effect of 100 nM sCAR nearly 3-fold. Such effects in other systems are due to nonessential activating cofactors. IMPORTANCE A factor other than the virus receptor expressed by target cells has been found to accelerate the loss of an enterovirus (CVB3/28) infectious titer, with little effect on nearly identical mutant strains. The destabilizing factor in fetal bovine serum, identified as albumin, does not interfere with the catalytic activity of soluble receptor at saturating receptor concentrations and amplifies the catalytic activity of the soluble receptor at a concentration that otherwise produces about one-third the saturated receptor-catalyzed rate of virus decay. This finding evidences the possibility that other virus-“priming” ligands may also be nonessential activating cofactors that serve to accelerate receptor-catalyzed viral eclipse.

Original languageEnglish (US)
Article numbere0196219
JournalJournal of virology
Volume94
Issue number6
DOIs
StatePublished - Mar 1 2020

Keywords

  • Coxsackievirus
  • Enterovirus
  • Kinetics
  • Receptor
  • Uncoating

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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