Three-dimensional structure of vaccinia virus-produced human papillomavirus type 1 capsids.
The capsid proteins of papillomavirus self-assemble to form empty capsids or virus-like particles that appear quite similar to naturally occurring virions by conventional electron microscopy. To characterize such virus-like particles more fully, cryoelectron microscopy and image analysis techniques were used to generate three-dimensional reconstructions of capsids produced by vaccinia virus recombinants (V capsids) that expressed human papillomavirus type 1 L1 protein only or both L1 and L2 proteins. All V capsids had 72 pentameric capsomers arranged on a T = 7 icosahedral lattice. Each particle (approximately 60 nm in diameter) consisted of an approximately 2-nm-thick shell of protein with a radius of 22 nm with capsomers that extend approximately 6 nm from the shell. At a resolution of 3.5 nm, both V capsid structures appear identical to the capsid structure of native human papillomavirus type 1 (T. S. Baker, W. W. Newcomb, N. H. Olson, L. M. Cowsert, C. Olson, and J. C. Brown, Biophys. J. 60:1445-1456, 1991), thus implying that expressed and native capsids are structurally equivalent.
Hagensee
M E
ME
Program in Cancer Biology, Fred Hutchinson Cancer Research Center, Seattle, Washington 98104-2092.
Olson
N H
NH
Baker
T S
TS
Galloway
D A
DA
D002213:Capsid / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D003001:Cloning, Molecular; D008854:Microscopy, Electron / Q000379:methods; D027383:Papillomaviridae / Q000648:ultrastructure*; D010316:Particle Size; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000648:ultrastructure; D014616:Vaccinia virus / Q000235:genetics*
D011994:Recombinant Proteins