title: Maturation of phage T7 involves structural modification of both shell and inner core components.
abstract: The double-stranded DNA bacteriophages are good model systems to understand basic biological processes such as the macromolecular interactions that take place during the virus assembly and maturation, or the behavior of molecular motors that function during the DNA packaging process. Using cryoelectron microscopy and single-particle methodology, we have determined the structures of two phage T7 assemblies produced during its morphogenetic process, the DNA-free prohead and the mature virion. The first structure reveals a complex assembly in the interior of the capsid, which involves the scaffolding, and the core complex, which plays an important role in DNA packaging and is located in one of the phage vertices. The reconstruction of the mature virion reveals important changes in the shell, now much larger and thinner, the disappearance of the scaffolding structure, and important rearrangements of the core complex, which now protrudes the shell and interacts with the tail. Some of these changes must originate by the pressure exerted by the DNA in the interior of the head.
authors.affiliation: Centro Nacional de Biotecnología, Campus de la Universidad Autónoma de Madrid, Cantoblanco, Madrid, Spain.
authors.forename: Xabier
authors.initials: X
authors.lastname: Agirrezabala
authors.forename: Jaime
authors.initials: J
authors.lastname: Martín-Benito
authors.forename: José R
authors.initials: JR
authors.lastname: Castón
authors.forename: Roberto
authors.initials: R
authors.lastname: Miranda
authors.forename: José María
authors.initials: JM
authors.lastname: Valpuesta
authors.forename: José L
authors.initials: JL
authors.lastname: Carrascosa
mesh_terms: D017123:Bacteriophage T7 / Q000502:physiology* / Q000648:ultrastructure*; D002213:Capsid / Q000648:ultrastructure; D036022:Capsid Proteins / Q000648:ultrastructure; D020285:Cryoelectron Microscopy; D042003:DNA Packaging; D008958:Models, Molecular; D011487:Protein Conformation; D014764:Viral Proteins / Q000648:ultrastructure; D014771:Virion / Q000502:physiology* / Q000648:ultrastructure*; D019065:Virus Assembly
chemical_list: D036022:Capsid Proteins; D014764:Viral Proteins