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Cryo-electron microscopy structure of adenovirus type 2 temperature-sensitive mutant 1 reveals insight into the cell entry defect

Academic Article
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Overview

authors

  • Silvestry, M.
  • Lindert, S.
  • Smith, J. G.
  • Maier, O.
  • Wiethoff, C. M.
  • Nemerow, Glen
  • Stewart, P. L.

publication date

  • August 2009

journal

  • Journal of Virology  Journal

abstract

  • The structure of the adenovirus type 2 temperature-sensitive mutant 1 (Ad2ts1) was determined to a resolution of 10 A by cryo-electron microscopy single-particle reconstruction. Ad2ts1 was prepared at a nonpermissive temperature and contains the precursor forms of the capsid proteins IIIa, VI, and VIII; the core proteins VII, X (mu), and terminal protein (TP); and the L1-52K protein. Cell entry studies have shown that although Ad2ts1 can bind the coxsackievirus and Ad receptor and undergo internalization via alphav integrins, this mutant does not escape from the early endosome and is targeted for degradation. Comparison of the Ad2ts1 structure to that of mature Ad indicates that Ad2ts1 has a different core architecture. The Ad2ts1 core is closely associated with the icosahedral capsid, a connection which may be mediated by preproteins IIIa and VI. Density within hexon cavities is assigned to preprotein VI, and membrane disruption assays show that hexon shields the lytic activity of both the mature and precursor forms of protein VI. The internal surface of the penton base in Ad2ts1 appears to be anchored to the core by interactions with preprotein IIIa. Our structural analyses suggest that these connections to the core inhibit the release of the vertex proteins and lead to the cell entry defect of Ad2ts1.

subject areas

  • Adenoviridae
  • Adenoviridae Infections
  • Capsid
  • Cell Line
  • Cryoelectron Microscopy
  • Humans
  • Mutation
  • Temperature
  • Viral Proteins
  • Virion
  • Virus Assembly
  • Virus Internalization
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Identity

PubMed Central ID

  • PMC2708647

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/jvi.00331-09

PubMed ID

  • 19458007
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Additional Document Info

start page

  • 7375

end page

  • 7383

volume

  • 83

issue

  • 15

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