Crystal Structure of Human Adenovirus at 3.5 Å Resolution

Journal Article · Mon Sep 27 04:00:00 EDT 2010 · Science

DOI:https://doi.org/10.1126/science.1187292· OSTI ID:1002699

Reddy, Vijay S; Natchiar, S Kundhavai; Stewart, Phoebe L; Nemerow, Glen R ^[1]

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1. Scripps

Rational development of adenovirus vectors for therapeutic gene transfer is hampered by the lack of accurate structural information. Here, we report the x-ray structure at 3.5 angstrom resolution of the 150-megadalton adenovirus capsid containing nearly 1 million amino acids. We describe interactions between the major capsid protein (hexon) and several accessory molecules that stabilize the capsid. The virus structure also reveals an altered association between the penton base and the trimeric fiber protein, perhaps reflecting an early event in cell entry. The high-resolution structure provides a substantial advance toward understanding the assembly and cell entry mechanisms of a large double-stranded DNA virus and provides new opportunities for improving adenovirus-mediated gene transfer.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: USDOE
• OSTI ID: 1002699
• Journal Information: Science, Journal Name: Science Journal Issue: 08, 2010 Vol. 329; ISSN 0193-4511; ISSN SCEHDK
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

36 MATERIALS SCIENCE
ADENOVIRUS
AMINO ACIDS
CRYSTAL STRUCTURE
DNA
FIBERS
GENES
PROTEINS
RESOLUTION
VECTORS