Variations of coxsackievirus B3 capsid primary structure, ligands, and stability are selected for in a coxsackievirus and adenovirus receptor-limited environment

Steven D Carson, Nora M Chapman, Susan Hafenstein, Steven M Tracy

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

While group B coxsackieviruses (CVB) use the coxsackievirus and adenovirus receptor (CAR) as the receptor through which they infect susceptible cells, some CVB strains are known for their acquired capacity to bind other molecules. The CVB3/RD strain that emerged from a CVB3/Nancy population sequentially passaged in the CAR-poor RD cell line binds decay-accelerating factor (DAF) (CD55) and CAR. A new strain, CVB3/RDVa, has been isolated from RD cells chronically infected with CVB3/RD and binds multiple molecules in addition to DAF and CAR. The capsid proteins of CVB3/RD differ from those of CVB3/28, a cloned strain that binds only CAR, by only four amino acids, including a glutamate/ glutamine dimorphism in the DAF-binding region of the capsid. The capsid proteins of CVB3/RD and CVB3/RDVa differ by seven amino acids. The ability of CVB3/RDVa to bind ligands in addition to CAR and DAF may be attributed to lysine residues near the icosahedral 5-fold axes of symmetry. Considered with differences in the stability of the CVB3 strains, these traits suggest that in vitro selection in a CAR-limited environment selects for virus populations that can associate with molecules on the cell surface and survive until CAR becomes available to support infection.

Original languageEnglish (US)
Pages (from-to)3306-3314
Number of pages9
JournalJournal of virology
Volume85
Issue number7
DOIs
StatePublished - Apr 1 2011

Fingerprint

Enterovirus
capsid
Capsid
Adenoviridae
CD55 Antigens
Ligands
receptors
deterioration
Capsid Proteins
coat proteins
Human Enterovirus B
Amino Acids
ligands
adenovirus receptor
amino acids
Glutamine
cells
Population
Lysine
dimorphism

ASJC Scopus subject areas

  • Immunology
  • Virology

Cite this

Variations of coxsackievirus B3 capsid primary structure, ligands, and stability are selected for in a coxsackievirus and adenovirus receptor-limited environment. / Carson, Steven D; Chapman, Nora M; Hafenstein, Susan; Tracy, Steven M.

In: Journal of virology, Vol. 85, No. 7, 01.04.2011, p. 3306-3314.

Research output: Contribution to journalArticle

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