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Integrin-alpha-v-beta-3 and integrin-alpha-v-beta-5 promote adenovirus internalization but not virus attachment

Academic Article
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Overview

authors

  • Wickham, T. J.
  • Mathias, P.
  • Cheresh, D. A.
  • Nemerow, Glen

publication date

  • April 1993

journal

  • Cell  Journal

abstract

  • Adenovirus contains a heterodimeric protein complex consisting of 186 kd fiber protein that mediates high affinity virus attachment to cells and a 400 kd pentavalent subunit (penton base) that contains five Arg-Gly-Asp sequences, implying a role for integrins in adenovirus infection. We demonstrate that the vitro-nectin-binding integrins alpha v beta 3 and alpha v beta 5 promote viral infection in a novel way since antibodies against these receptors or soluble penton base block virus internalization without affecting attachment. Moreover, adenovirus binds to cultured cells lacking alpha v integrins but fail to become internalized, thus restricting infection of these cells. Transfection of alpha v(-) cells with a cDNA encoding alpha v results in the expression of integrins alpha v beta 3 and alpha v beta 5 and allows virus internalization and infection. These data indicate that adenovirus attachment and uptake into cells are separate but cooperative events that result from the interaction of distinct viral coat proteins with a receptor for attachment and alpha v integrin receptors for internalization.

subject areas

  • Adenoviruses, Human
  • Amino Acid Sequence
  • Capsid
  • Capsid Proteins
  • Cell Adhesion
  • Endocytosis
  • Extracellular Matrix
  • HeLa Cells
  • Humans
  • In Vitro Techniques
  • Integrins
  • Molecular Sequence Data
  • Oligopeptides
  • Receptors, Virus
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Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/0092-8674(93)90231-e

PubMed ID

  • 8477447
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Additional Document Info

start page

  • 309

end page

  • 319

volume

  • 73

issue

  • 2

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