Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 1 - 14 |
| Number of pages | 14 |
| Journal | PLoS Pathogens |
| Volume | 7 |
| Issue number | 9 (e1002239) |
| DOIs | |
| Publication status | Published - 2011 |
Cite this
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Membrane remodeling by the double-barrel scaffolding protein of poxvirus. / Hyun, Jae-Kyung; Accurso, Cathy; Hijnen, Marcel; Schult, Philipp; Pettikiriarachchi, Anne; Mitra, Alok; Coulibaly, Fasseli.
In: PLoS Pathogens, Vol. 7, No. 9 (e1002239), 2011, p. 1 - 14.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - Membrane remodeling by the double-barrel scaffolding protein of poxvirus
AU - Hyun, Jae-Kyung
AU - Accurso, Cathy
AU - Hijnen, Marcel
AU - Schult, Philipp
AU - Pettikiriarachchi, Anne
AU - Mitra, Alok
AU - Coulibaly, Fasseli
PY - 2011
Y1 - 2011
N2 - In contrast to most enveloped viruses, poxviruses produce infectious particles that do not acquire their internal lipid membrane by budding through cellular compartments. Instead, poxvirus immature particles are generated from atypical crescent-shaped precursors whose architecture and composition remain contentious. Here we describe the 2.6 A crystal structure of vaccinia virus D13, a key structural component of the outer scaffold of viral crescents. D13 folds into two jellyrolls decorated by a head domain of novel fold. It assembles into trimers that are homologous to the double-barrel capsid proteins of adenovirus and lipid-containing icosahedral viruses. We show that, when tethered onto artificial membranes, D13 forms a honeycomb lattice and assembly products structurally similar to the viral crescents and immature particles. The architecture of the D13 honeycomb lattice and the lipid-remodeling abilities of D13 support a model of assembly that exhibits similarities with the giant mimivirus. Overall, these findings establish that the first committed step of poxvirus morphogenesis utilizes an ancestral lipid-remodeling strategy common to icosahedral DNA viruses infecting all kingdoms of life. Furthermore, D13 is the target of rifampicin and its structure will aid the development of poxvirus assembly inhibitors.
AB - In contrast to most enveloped viruses, poxviruses produce infectious particles that do not acquire their internal lipid membrane by budding through cellular compartments. Instead, poxvirus immature particles are generated from atypical crescent-shaped precursors whose architecture and composition remain contentious. Here we describe the 2.6 A crystal structure of vaccinia virus D13, a key structural component of the outer scaffold of viral crescents. D13 folds into two jellyrolls decorated by a head domain of novel fold. It assembles into trimers that are homologous to the double-barrel capsid proteins of adenovirus and lipid-containing icosahedral viruses. We show that, when tethered onto artificial membranes, D13 forms a honeycomb lattice and assembly products structurally similar to the viral crescents and immature particles. The architecture of the D13 honeycomb lattice and the lipid-remodeling abilities of D13 support a model of assembly that exhibits similarities with the giant mimivirus. Overall, these findings establish that the first committed step of poxvirus morphogenesis utilizes an ancestral lipid-remodeling strategy common to icosahedral DNA viruses infecting all kingdoms of life. Furthermore, D13 is the target of rifampicin and its structure will aid the development of poxvirus assembly inhibitors.
UR - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=21931553
U2 - 10.1371/journal.ppat.1002239
DO - 10.1371/journal.ppat.1002239
M3 - Article
VL - 7
SP - 1
EP - 14
JO - PLoS Pathogens
JF - PLoS Pathogens
SN - 1553-7366
IS - 9 (e1002239)
ER -