PXD015941-3

PXD015941 is an original dataset announced via ProteomeXchange.

Title	Structure of herpes simplex virus pUL7:pUL51, a conserved complex required for efficient herpesvirus assembly
Description	Herpesviruses are an ancient family of highly-prevalent human and animal pathogens that acquire their membrane envelopes in the cytoplasm of infected cells. While multiple conserved viral proteins are known to be required for efficient herpesvirus production, many of these proteins lack identifiable structural homologues and the molecular details of herpesvirus assembly remain unclear. We have characterized the complex of assembly proteins pUL7 and pUL51 from herpes simplex virus (HSV)-1, an α-herpesvirus, using multi-angle light scattering and small-angle X-ray scattering with chemical crosslinking. HSV-1 pUL7 and pUL51 form a stable 1:2 complex that is capable of higher-order oligomerization in solution. We solved the crystal structure of this complex, revealing a core heterodimer comprising pUL7 bound to residues 41–125 of pUL51. While pUL7 adopts a previously-unseen compact fold, the extended helix-turn-helix conformation of pUL51 resembles the cellular endosomal complex required for transport (ESCRT)- III component CHMP4B, suggesting a direct role for pUL51 in promoting membrane scission during virus assembly. We demonstrate that the interaction between pUL7 and pUL51 homologues is conserved acrosshuman α-, β- and γ-herpesviruses, as is their association with trans-Golgi membranes in cultured cells. However, pUL7 and pUL51 homologues do not form complexes with their respective partners from different virus families, suggesting that the molecular details of the interaction interface have diverged. Our results demonstrate that the pUL7:pUL51 complex is conserved across the herpesviruses and provide a structural framework for understanding its role in herpesvirus assembly.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:03:29.457.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Jack Houghton
SpeciesList	scientific name: Bacteria; NCBI TaxID: NCBITaxon:2; scientific name: Human alphaherpesvirus 1; NCBI TaxID: NCBITaxon:10298; scientific name: Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1); NCBI TaxID: 10306;
ModificationList	monohydroxylated residue; acetylated residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2019-10-21 06:41:57	ID requested
1	2020-05-11 07:42:50	announced
2	2020-07-22 06:55:28	announced	2020-07-22: Updated publication reference for PubMed record(s): 32391791.
⏵ 3	2024-10-22 05:03:32	announced	2024-10-22: Updated project metadata.

10.7554/elife.53789;

Butt BG, Owen DJ, Jeffries CM, Ivanova L, Hill CH, Houghton JW, Ahmed MF, Antrobus R, Svergun DI, Welch JJ, Crump CM, Graham SC, Insights into herpesvirus assembly from the structure of the pUL7:pUL51 complex. Elife, 9():(2020) [pubmed]

submitter keyword: Secondary envelopment

virus budding

focal adhesions

human cytomegalovirus (HCMV)

Dr Stephen C Graham
contact affiliation	Department of Pathology, University of Cambridge
contact email	scg34@cam.ac.uk
lab head
Jack Houghton
contact affiliation	University of Cambridge
contact email	jwh65@cam.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD015941
     1. Label: PRIDE project
     2. Name: Structure of herpes simplex virus pUL7:pUL51, a conserved complex required for efficient herpesvirus assembly