8bbt
Native Tipula oleracea Nudivirus polyhedrin - 1960Native Tipula oleracea Nudivirus polyhedrin - 1960
Structural highlights
FunctionPublication Abstract from PubMedInfectious protein crystals are an essential part of the viral lifecycle for double-stranded DNA Baculoviridae and double-stranded RNA cypoviruses. These viral protein crystals, termed occlusion bodies or polyhedra, are dense protein assemblies that form a crystalline array, encasing newly formed virions. Here, using X-ray crystallography we determine the structure of a polyhedrin from Nudiviridae. This double-stranded DNA virus family is a sister-group to the baculoviruses, whose members were thought to lack occlusion bodies. The 70-year-old sample contains a well-ordered lattice formed by a predominantly alpha-helical building block that assembles into a dense, highly interconnected protein crystal. The lattice is maintained by extensive hydrophobic and electrostatic interactions, disulfide bonds, and domain switching. The resulting lattice is resistant to most environmental stresses. Comparison of this structure to baculovirus or cypovirus polyhedra shows a distinct protein structure, crystal space group, and unit cell dimensions, however, all polyhedra utilise common principles of occlusion body assembly. Atomic structure of a nudivirus occlusion body protein determined from a 70-year-old crystal sample.,Keown JR, Crawshaw AD, Trincao J, Carrique L, Gildea RJ, Horrell S, Warren AJ, Axford D, Owen R, Evans G, Bezier A, Metcalf P, Grimes JM Nat Commun. 2023 Jul 13;14(1):4160. doi: 10.1038/s41467-023-39819-1. PMID:37443157[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||