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A correction was published on 19 December 2012, see Viruses 2012, 4(12), 3952.

Viruses 2012, 4(5), 847-877; doi:10.3390/v4050847
Review

Latest Insights on Adenovirus Structure and Assembly

Received: 18 April 2012; Accepted: 11 May 2012 / Published: 21 May 2012
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Abstract: Adenovirus (AdV) capsid organization is considerably complex, not only because of its large size (~950 Å) and triangulation number (pseudo T = 25), but also because it contains four types of minor proteins in specialized locations modulating the quasi-equivalent icosahedral interactions. Up until 2009, only its major components (hexon, penton, and fiber) had separately been described in atomic detail. Their relationships within the virion, and the location of minor coat proteins, were inferred from combining the known crystal structures with increasingly more detailed cryo-electron microscopy (cryoEM) maps. There was no structural information on assembly intermediates. Later on that year, two reports described the structural differences between the mature and immature adenoviral particle, starting to shed light on the different stages of viral assembly, and giving further insights into the roles of core and minor coat proteins during morphogenesis [1,2]. Finally, in 2010, two papers describing the atomic resolution structure of the complete virion appeared [3,4]. These reports represent a veritable tour de force for two structural biology techniques: X-ray crystallography and cryoEM, as this is the largest macromolecular complex solved at high resolution by either of them. In particular, the cryoEM analysis provided an unprecedented clear picture of the complex protein networks shaping the icosahedral shell. Here I review these latest developments in the field of AdV structural studies.
Keywords: adenovirus; structure; maturation; minor coat proteins; core proteins; cryo-electron microscopy; crystallography adenovirus; structure; maturation; minor coat proteins; core proteins; cryo-electron microscopy; crystallography
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
  • Correction

    A correction was published on 19 December 2012: http://www.mdpi.com/1999-4915/4/12/3952 (PDF, 16 KB)

    It has come to my attention that my article "Latest Insights on Adenovirus Structure and Assembly" (Viruses 2012, 4, 847-877) [1] contains an inaccurate statement. On page 864, the caption for Figure 7 reads: "There are four potential cleavage sites in pTP but they have not been experimentally verified". However, three of these sites have been experimentally confirmed in vitro using recombinant AVP and pTP, as described in Webster A, Leith I.R., Hay R.T.: Activation of adenovirus-coded protease and processing of preterminal protein. J. Virol. 1994, 68, 7292-7300 [2].

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MDPI and ACS Style

San Martín, C. Latest Insights on Adenovirus Structure and Assembly. Viruses 2012, 4, 847-877.

AMA Style

San Martín C. Latest Insights on Adenovirus Structure and Assembly. Viruses. 2012; 4(5):847-877.

Chicago/Turabian Style

San Martín, Carmen. 2012. "Latest Insights on Adenovirus Structure and Assembly." Viruses 4, no. 5: 847-877.



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