Implications for viral uncoating from the structure of bovine enterovirus.
We have determined the crystal structure of a bovine enterovirus, revealing that the topologies of the major capsid proteins and the overall architecture of the virion are similar to those of related picornaviruses. The external loops joining beta-strands are truncated and the canyon region is partially filled by an extension of the VP3 G-H loop giving the viral capsid a relatively smooth appearance. These changes may have implications for cell attachment. In spite of these differences the virus maintains a hydrophobic pocket within VP1, occupied by a specific 'pocket factor' which appears to be myristic acid. These observations support the proposal that a kinetic equilibrium exists between occupied and unoccupied pocket states, with occupation inhibiting uncoating.
Smyth
M
M
Laboratory of Molecular Biophysics, Oxford, UK.
Tate
J
J
Hoey
E
E
Lyons
C
C
Martin
S
S
Stuart
D
D
D000818:Animals; D002213:Capsid / Q000737:chemistry*; D036022:Capsid Proteins; D002417:Cattle; D003460:Crystallization; D004770:Enterovirus / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D010849:Picornaviridae / Q000737:chemistry; D011487:Protein Conformation
D036022:Capsid Proteins