Related Experiment Video

Updated: Mar 31, 2026

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
06:40

Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy

Published on: November 4, 2018

6.7K

Structural basis of membrane budding by the nuclear egress complex of herpesviruses

Janna M Bigalke1, Ekaterina E Heldwein2

  • 1Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA, USA.

The EMBO Journal
|October 30, 2015
PubMed

Insights

Herpesvirus nuclear egress complex (NEC) proteins UL31 and UL34 form a honeycomb lattice to drive viral particle budding from the nuclear membrane. This structural insight reveals the mechanism of viral nuclear egress and potential targets for antiviral drugs.

Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • Herpesvirus nuclear egress involves capsid budding at the inner nuclear membrane, mediated by the nuclear egress complex (NEC) comprising UL31 and UL34 proteins.
  • Previous studies showed NEC can bud synthetic membranes in vitro by forming a hexagonal scaffold.

Purpose of the Study:

  • To elucidate the structural basis of NEC-mediated membrane budding.
  • To understand the mechanism of herpesvirus nuclear egress.

Main Methods:

  • Determined crystal structures of the NEC from two herpesviruses.
  • Performed mutagenesis to perturb oligomeric interfaces.
  • Assessed budding efficiency in vitro.

Main Results:

  • Observed hexagonal lattice structures in NEC crystals, recapitulating honeycomb coats in budded vesicles.
  • Mutagenesis of oligomeric interfaces blocked in vitro budding.
  • Confirmed NEC oligomerization into a honeycomb lattice drives membrane budding.

Conclusions:

  • NEC oligomerization into a honeycomb lattice is the driving force for membrane budding during herpesvirus nuclear egress.
  • The atomic-level structure provides a framework for dissecting the budding mechanism.
  • This understanding facilitates the design of novel antiviral inhibitors targeting NEC function.
Keywords:
UL31UL34herpesvirusmembrane buddingnuclear egress

More Related Videos

Live Cell Imaging of Alphaherpes Virus Anterograde Transport and Spread15:31

Live Cell Imaging of Alphaherpes Virus Anterograde Transport and Spread

Published on: August 16, 2013

11.6K
Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins08:26

Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins

Published on: August 31, 2017

14.3K

Related Concept Videos

Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
4.4K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
3.4K
Intracellular Movement of Viruses and Bacteria01:10

Intracellular Movement of Viruses and Bacteria

Intracellular bacteria and viruses often comprise a group of highly infectious pathogens that can cause several diseases. Bacterial pathogens include those belonging to the genus Rickettsia responsible for conditions such as rocky mountain spotted fever and the Mediterranean spotted fever; Chlamydia, a genus responsible for a sexually transmitted disease; Coxiella burnetii, an agent responsible for Q fever. Viral pathogens include vaccinia—a poxvirus, and herpes simplex virus—a...
3.8K
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
5.2K
Nuclear Export of mRNA02:31

Nuclear Export of mRNA

Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...
9.2K
Nuclear Export of mRNA02:31

Nuclear Export of mRNA

5.6K