The concerted conformational changes during human rhinovirus 2 uncoating.
Delivery of the rhinovirus genome into the cytoplasm involves a cooperative structural modification of the viral capsid. We have studied this phenomenon for human rhinovirus serotype 2 (HRV2). The structure of the empty capsid has been determined to a resolution of better than 15 A by cryo-electron microscopy, and the atomic structure of native HRV2 was used to examine conformational changes of the capsid. The two proteins around the 5-fold axes make an iris type of movement to open a 10 A diameter channel which allows the RNA genome to exit, and the N terminus of VP1 exits the capsid at the pseudo 3-fold axis. A remarkable modification occurs at the 2-fold axes where the N-terminal loop of VP2 bends inward, probably to detach the RNA.
Institut de Biologie Structurale Jean-Pierre Ebel, 41 rue Jules Horowitz, 38027 Grenoble, France. hewat@ibs.fr
Elizabeth A
EA
Hewat
Emmanuelle
E
Neumann
Dieter
D
Blaas
D002213:Capsid / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D012367:RNA, Viral / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D012229:Rhinovirus / Q000235:genetics / Q000254:growth & development / Q000378:metabolism* / Q000648:ultrastructure*; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure
D012367:RNA, Viral; D014764:Viral Proteins