Coxsackievirus and adenovirus receptor amino-terminal immunoglobulin V- related domain binds adenovirus type 2 and fiber knob from adenovirus type 12

Paul Freimuth, Karen Springer, Chris Berard, Jim Hainfeld, Maria Bewley, John Flanagan

Research output: Contribution to journalArticle

98 Citations (Scopus)

Abstract

The extracellular region of the coxsackievirus and adenovirus receptor (CAR) is predicted to consist of two immunoglobulin (Ig)-related structural domains. We expressed the isolated CAR amino-terminal domain (D1) and a CAR fragment containing both extracellular Ig domains (D1/D2) in Escherichia coli. Both D1 and D1/D2 formed complexes in vitro with the recombinant knob domain of adenovirus type 12 (Ad12) fiber, and D1 inhibited adenovirus type 2 (Ad2) infection of HeLa cells. These results indicate that the adenovirus- binding activity of CAR is localized in the amino-terminal IgV-related domain and confirm our earlier observation that Ad2 and Ad12 bind to the same cellular receptor. Preliminary crystallization studies suggest that complexes of Ad12 knob bound to D1 will be suitable for structure determination.

Original languageEnglish (US)
Pages (from-to)1392-1398
Number of pages7
JournalJournal of virology
Volume73
Issue number2
StatePublished - Jan 23 1999

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Immunoglobulin Variable Region
Enterovirus
Adenoviridae
immunoglobulins
receptors
Adenoviridae Infections
Crystallization
HeLa Cells
Immunoglobulins
adenovirus receptor
Escherichia coli
crystallization

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Cite this

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Coxsackievirus and adenovirus receptor amino-terminal immunoglobulin V- related domain binds adenovirus type 2 and fiber knob from adenovirus type 12. / Freimuth, Paul; Springer, Karen; Berard, Chris; Hainfeld, Jim; Bewley, Maria; Flanagan, John.

In: Journal of virology, Vol. 73, No. 2, 23.01.1999, p. 1392-1398.

Research output: Contribution to journalArticle

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AU - Freimuth, Paul

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