Adenovirus structure.
Structural studies continue to play an essential role as the focus of adenovirus research shifts in emphasis from basic biology to adenovirus-based vector technologies. A crucial step in developing novel therapeutics for gene replacement, cancer, and vaccines is often to modify the virion. Such engineered changes are designed to retarget the virus, or to reduce the immunological responses to infection. These efforts are far more effective when they are based on detailed structural knowledge. This minireview provides a brief summary of the wealth of information that has been obtained from the combined application of X-ray crystallography and electron microscopy. This knowledge now includes a good working model for the architectural organization of the virion, and atomic resolution molecular structures for all the major capsid proteins, hexon, penton, and fiber. We highlight new developments, which include the structure of the penton base and the discovery that adenovirus has several relatives. We sketch how the structural information can be used to engineer novel virions and conclude with the prospects for future progress.
Rux
John J
JJ
The Wistar Institute, Philadelphia, PA 19104, USA.
Burnett
Roger M
RM
D000260:Adenoviruses, Human / Q000737:chemistry* / Q000648:ultrastructure; D036022:Capsid Proteins / Q000737:chemistry / Q000648:ultrastructure; D018360:Crystallography, X-Ray; D005544:Forecasting; D006801:Humans; D008854:Microscopy, Electron; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D017361:Viral Nonstructural Proteins / Q000737:chemistry; D015678:Viral Structural Proteins / Q000737:chemistry; D014771:Virion / Q000737:chemistry / Q000648:ultrastructure
D036022:Capsid Proteins; D017361:Viral Nonstructural Proteins; D015678:Viral Structural Proteins; C018315:hexon capsid protein, Adenovirus; C043322:penton protein, adenovirus