6q1f | pdb_00006q1f
Atomic structure of the Human Herpesvirus 6B Capsid and Capsid-Associated Tegument Complexes
Structural highlights
Function[TRX1_HHV6Z] Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly. [MCP_HHV6Z] Self-assembles to form an icosahedral capsid with a T=16 symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12 pentons (total of 162 capsomers). Hexons form the edges and faces of the capsid and are each composed of six MCP molecules. In contrast, one penton is found at each of the 12 vertices. Eleven of the pentons are MCP pentamers, while the last vertex is occupied by the portal complex. The capsid is surrounded by a layer of proteinaceous material designated the tegument which, in turn, is enclosed in an envelope of host cell-derived lipids containing virus-encoded glycoproteins. [SCP_HHV6Z] Participates in the assembly of the infectious particles by decorating the outer surface of the capsid shell and thus forming a layer between the capsid and the tegument. Complexes composed of the major capsid protein and small capsomere-interacting protein/SCP assemble together in the host cytoplasm and are translocated to the nucleus, where they accumulate and participate in capsid assembly. [TRX2_HHV6Z] Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly. Publication Abstract from PubMedHuman herpesvirus 6B (HHV-6B) belongs to the beta-herpesvirus subfamily of the Herpesviridae. To understand capsid assembly and capsid-tegument interactions, here we report atomic structures of HHV-6B capsid and capsid-associated tegument complex (CATC) obtained by cryoEM and sub-particle reconstruction. Compared to other beta-herpesviruses, HHV-6B exhibits high similarity in capsid structure but organizational differences in its CATC (pU11 tetramer). 180 "VLambda"-shaped CATCs are observed in HHV-6B, distinguishing from the 255 "Lambda"-shaped dimeric CATCs observed in murine cytomegalovirus and the 310 "Delta"-shaped CATCs in human cytomegalovirus. This trend in CATC quantity correlates with the increasing genomes sizes of these beta-herpesviruses. Incompatible distances revealed by the atomic structures rationalize the lack of CATC's binding to triplexes Ta, Tc, and Tf in HHV-6B. Our results offer insights into HHV-6B capsid assembly and the roles of its tegument proteins, including not only the beta-herpesvirus-specific pU11 and pU14, but also those conserved across all subfamilies of Herpesviridae. Atomic structure of the human herpesvirus 6B capsid and capsid-associated tegument complexes.,Zhang Y, Liu W, Li Z, Kumar V, Alvarez-Cabrera AL, Leibovitch EC, Cui Y, Mei Y, Bi GQ, Jacobson S, Zhou ZH Nat Commun. 2019 Nov 25;10(1):5346. doi: 10.1038/s41467-019-13064-x. PMID:31767868[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||
