Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks.
Construction of a complex virus may involve a hierarchy of assembly elements. Here, we report the structure of the whole human adenovirus virion at 3.6 angstroms resolution by cryo-electron microscopy (cryo-EM), revealing in situ atomic models of three minor capsid proteins (IIIa, VIII, and IX), extensions of the (penton base and hexon) major capsid proteins, and interactions within three protein-protein networks. One network is mediated by protein IIIa at the vertices, within group-of-six (GOS) tiles--a penton base and its five surrounding hexons. Another is mediated by ropes (protein IX) that lash hexons together to form group-of-nine (GON) tiles and bind GONs to GONs. The third, mediated by IIIa and VIII, binds each GOS to five surrounding GONs. Optimization of adenovirus for cancer and gene therapy could target these networks.
Liu
Hongrong
H
Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles (UCLA), Los Angeles, CA 90095-7364, USA.
Jin
Lei
L
Koh
Sok Boon S
SB
Atanasov
Ivo
I
Schein
Stan
S
Wu
Lily
L
Zhou
Z Hong
ZH
D000260:Adenoviruses, Human / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure*; D002213:Capsid / Q000737:chemistry / Q000648:ultrastructure; D036022:Capsid Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D020285:Cryoelectron Microscopy; D016679:Genome, Viral; D007091:Image Processing, Computer-Assisted; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D014771:Virion / Q000737:chemistry / Q000648:ultrastructure
D036022:Capsid Proteins; C018315:hexon capsid protein, Adenovirus; C043322:penton protein, adenovirus
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