Publication Date:
2008-05-02
Description:
Cytoplasmic polyhedrosis virus (CPV) is unique within the Reoviridae family in having a turreted single-layer capsid contained within polyhedrin inclusion bodies, yet being fully capable of cell entry and endogenous RNA transcription. Biochemical data have shown that the amino-terminal 79 residues of the CPV turret protein (TP) is sufficient to bring CPV or engineered proteins into the polyhedrin matrix for micro-encapsulation. Here we report the three-dimensional structure of CPV at 3.88 A resolution using single-particle cryo-electron microscopy. Our map clearly shows the turns and deep grooves of alpha-helices, the strand separation in beta-sheets, and densities for loops and many bulky side chains; thus permitting atomic model-building effort from cryo-electron microscopy maps. We observed a helix-to-beta-hairpin conformational change between the two conformational states of the capsid shell protein in the region directly interacting with genomic RNA. We have also discovered a messenger RNA release hole coupled with the mRNA capping machinery unique to CPV. Furthermore, we have identified the polyhedrin-binding domain, a structure that has potential in nanobiotechnology applications.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2746981/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2746981/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, Xuekui -- Jin, Lei -- Zhou, Z Hong -- P41 RR002250/RR/NCRR NIH HHS/ -- P41 RR002250-190043/RR/NCRR NIH HHS/ -- P41 RR002250-200043/RR/NCRR NIH HHS/ -- P41 RR002250-217385/RR/NCRR NIH HHS/ -- P41 RR002250-226489/RR/NCRR NIH HHS/ -- R01 AI069015/AI/NIAID NIH HHS/ -- R01 AI069015-01A1/AI/NIAID NIH HHS/ -- R01 AI069015-02/AI/NIAID NIH HHS/ -- R01 AI069015-03/AI/NIAID NIH HHS/ -- R01 GM071940/GM/NIGMS NIH HHS/ -- R01 GM071940-01A2/GM/NIGMS NIH HHS/ -- R01 GM071940-02/GM/NIGMS NIH HHS/ -- R01 GM071940-03/GM/NIGMS NIH HHS/ -- R01 GM071940-04/GM/NIGMS NIH HHS/ -- England -- Nature. 2008 May 15;453(7193):415-9. doi: 10.1038/nature06893. Epub 2008 Apr 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Laboratory Medicine, The University of Texas Medical School at Houston, Houston, Texas 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18449192" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Bombyx/virology
;
Capsid Proteins/chemistry/ultrastructure
;
*Cryoelectron Microscopy
;
Genome, Viral/physiology
;
Larva/virology
;
Models, Molecular
;
RNA Caps/genetics/metabolism
;
RNA Transport
;
RNA, Viral/genetics/metabolism
;
Reoviridae/chemistry/genetics/metabolism/*ultrastructure
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
