한빛사논문
- 조회1,073
Jaekyung Hyun1,2,*, Hideyuki Matsunami1, Tae Gyun Kim1,4 & Matthias Wolf1,3,*
1Molecular Cryo-Electron Microscopy Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, 904-0495 Onna-son, Okinawa, Japan. 2Department of Convergence Medicine, School of Medicine, Pusan National University, 50612 Yangsan-si, Gyeongsangnamdo, Republic of Korea. 3Institute of Biological Chemistry, Academia Sinica, 128 Academia Road Sec. 2, 115 Taipei, Taiwan. 4Present address: Center for Vaccine Commercialization, R&D Planning Team, Gyeongbuk Institute for Bio Industry, 36618 Andong-si, Gyeongsanbukdo, Republic of Korea.
*Corresponding author.
Abstract
In Vaccinia virus (VACV), the prototype poxvirus, scaffold protein D13 forms a honeycomb-like lattice on the viral membrane that results in formation of the pleomorphic immature virion (IV). The structure of D13 is similar to those of major capsid proteins that readily form icosahedral capsids in nucleocytoplasmic large DNA viruses (NCLDVs). However, the detailed assembly mechanism of the nonicosahedral poxvirus scaffold has never been understood. Here we show the cryo-EM structures of the D13 trimer and scaffold intermediates produced in vitro. The structures reveal that the displacement of the short N-terminal α-helix is critical for initiation of D13 self-assembly. The continuous curvature of the IV is mediated by electrostatic interactions that induce torsion between trimers. The assembly mechanism explains the semiordered capsid-like arrangement of D13 that is distinct from icosahedral NCLDVs. Our structures explain how a single protein can self-assemble into different capsid morphologies and represent a local exception to the universal Caspar-Klug theory of quasi-equivalence.
논문정보
- Research article
- 2022년 03월 (BRIC 등록일 2022-04-04)
- 국내(교신)+국외 연구진
- 생명과학 > 구조생물 및 생물물리학
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