Atomic structure of the human herpesvirus 6B capsid and capsid-associated tegument complexes

Yibo Zhang, Wei Liu, Zihang Li, Vinay Kumar, Ana L. Alvarez-Cabrera, Emily C. Leibovitch, Yanxiang Cui, Ye Mei, Guo-Qiang Bi, Steve Jacobson and Z. Hong Zhou ()
Additional contact information
Yibo Zhang: University of Science and Technology of China (USTC)
Wei Liu: University of Science and Technology of China (USTC)
Zihang Li: University of California, Los Angeles (UCLA)
Vinay Kumar: University of California, Los Angeles (UCLA)
Ana L. Alvarez-Cabrera: University of California, Los Angeles (UCLA)
Emily C. Leibovitch: National Institutes of Health (NIH)
Yanxiang Cui: University of California, Los Angeles (UCLA)
Ye Mei: East China Normal University (ECNU)
Guo-Qiang Bi: University of Science and Technology of China (USTC)
Steve Jacobson: National Institutes of Health (NIH)
Z. Hong Zhou: University of California, Los Angeles (UCLA)

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: Abstract Human herpesvirus 6B (HHV-6B) belongs to the β-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 β-herpesviruses, HHV-6B exhibits high similarity in capsid structure but organizational differences in its CATC (pU11 tetramer). 180 “VΛ”-shaped CATCs are observed in HHV-6B, distinguishing from the 255 “Λ”-shaped dimeric CATCs observed in murine cytomegalovirus and the 310 “Δ”-shaped CATCs in human cytomegalovirus. This trend in CATC quantity correlates with the increasing genomes sizes of these β-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 β-herpesvirus-specific pU11 and pU14, but also those conserved across all subfamilies of Herpesviridae.

Date: 2019
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-019-13064-x Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13064-x

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-019-13064-x

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().