ADENOVIRUS INTERACTION WITH ITS CELLULAR RECEPTOR CAR. Metadata

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Title

  • Main Title ADENOVIRUS INTERACTION WITH ITS CELLULAR RECEPTOR CAR.

Creator

  • Author: Howitt, J.
    Creator Type: Personal
  • Author: Anderson, C. W.
    Creator Type: Personal
  • Author: Freimuth, P.
    Creator Type: Personal

Contributor

  • Sponsor: United States. Department of Energy. Office of Energy Research.
    Contributor Type: Organization
    Contributor Info: USDOE Office of Energy Research (ER) (United States)

Publisher

  • Name: Brookhaven National Laboratory
    Place of Publication: Upton, New York
    Additional Info: Brookhaven National Lab., Upton, NY (United States)

Date

  • Creation: 2001-08

Language

  • English

Description

  • Content Description: The mechanism of adenovirus attachment to the host cell plasma membrane has been revealed in detail by research over the past 10 years. It has long been known that receptor binding activity is associated with the viral fibers, trimeric spike proteins that protrude radially from the vertices of the icosahedral capsid (Philipson et al. 1968). In some adenovirus serotypes, fiber and other virus structural proteins are synthesized in excess and accumulate in the cell nucleus during late stages of infection. Fiber protein can be readily purified from lysates of cells infected with subgroup C viruses, for example Ad2 and Ad5 (Boulanger and Puvion 1973). Addition of purified fiber protein to virus suspensions during adsorption strongly inhibits infection, indicating that fiber and intact virus particles compete for binding sites on host cells (Philipson et al. 1968; Hautala et al. 1998). Cell binding studies using purified radiolabeled fiber demonstrated that fiber binds specifically and with high affinity to the cell plasma membrane, and that cell lines typically used for laboratory propagation of adenovirus have approximately 10{sup 4} high-affinity receptor sites per cell (Persson et al. 1985; Freimuth 1996). Similar numbers of high-affinity binding sites for radiolabeled intact virus particles also were observed (Seth et al. 1994).
  • Physical Description: 46 pages

Subject

  • Keyword: Viruses
  • Keyword: Membranes
  • Keyword: Fibers
  • STI Subject Categories: 59 Basic Biological Sciences
  • Keyword: Proteins
  • Keyword: Adsorption
  • Keyword: Adenovirus
  • Keyword: Affinity
  • STI Subject Categories: 60 Applied Life Sciences
  • Keyword: Plasma

Source

  • Other Information: PBD: 1 Aug 2001

Collection

  • Name: Office of Scientific & Technical Information Technical Reports
    Code: OSTI

Institution

  • Name: UNT Libraries Government Documents Department
    Code: UNTGD

Resource Type

  • Book

Format

  • Text

Identifier

  • Report No.: BNL--68839
  • Report No.: 400412000
  • Grant Number: AC02-98CH10886
  • Office of Scientific & Technical Information Report Number: 789786
  • Archival Resource Key: ark:/67531/metadc725173

Note

  • Display Note: Refer requests to OSTI, Office of Scientific and Technical Information, 175 Oak Ridge Turnpike, Oak Ridge, TN 37830 (US); OSTI as DE00789786
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