Abstract
A detailed structural analysis of the entire human adenovirus capsid has been stymied by the complexity and size of this 150 MDa macromolecular complex. Over the past 10 years, the steady improvements in viral genome manipulation concomitant with advances in crystallographic techniques and data processing software has allowed structure determination of this virus by X-ray diffraction at 3.5 resolution. The virus structure revealed the location, folds, and interactions of major and minor (cement proteins) on the inner and outer capsid surface. This new structural information sheds further light on the process of adenovirus capsid assembly and virus-host cell interactions.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 115-121 |
| Number of pages | 7 |
| Journal | Current Opinion in Virology |
| Volume | 2 |
| Issue number | 2 |
| DOIs | |
| State | Published - Apr 2012 |
| Externally published | Yes |
Bibliographical note
Funding Information:GM/CA CAT 23 ID-D, Argonne National Laboratories, Chicago Illinois, GUP beam time was used. GM/CA CAT has been funded in whole or partly with Federal funds from the National Cancer Institute ( Y1-CO-1020 ) and the National Institute of General Medical Sciences ( Y1-GM-1104 ). Use of the Advanced Photon Source was supported by the U.S. Department of Energy , Basic Energy Sciences , Office of Science , under contract No. DE-AC02-06CH11357 .
Funding Information:
This work was supported by NIH grants AI070771 to V.S.R., HL054352 and EY011431 to G.R.N. and AI042929 to P.L.S.